Available online at www.sciencedirect.
com
Endocytic traffic in animal cell cytokinesis
Guillaume Montagnac1,2, Arnaud Echard1,3 and Philippe Chavrier1,2
Cytokinesis is the final step of mitosis whereby two daughter
cells physically separate. It is initiated by the assembly of an
actomyosin contractile ring at the mitotic cell equator, which
constricts the cytoplasm between the two reforming nuclei
resulting in the formation of a narrow intercellular bridge filled
with central spindle microtubule bundles. Cytokinesis
terminates with the cleavage of the intercellular bridge in a
poorly understood process called abscission. Recent work has
highlighted the importance of membrane trafficking events
occurring from membrane compartments flanking the bridge to
the central midbody region. In particular, polarized delivery of
endocytic recycling membranes is essential for completion of
animal cell cytokinesis. Why endocytic traffic occurs within the
intercellular bridge remains largely mysterious and its
significance for cytokinesis will be discussed.
Address
1
Institut Curie, Centre de Recherche, F-75248 Paris, France
2 furrowing but rather affects abscission [2,10–
CNRS, UMR144, Membrane and Cytoskeleton Dynamics, 26 rue
d’Ulm, 75248 Paris Cedex 05, France
3
CNRS, UMR144, Molecular Mechanisms of Intracellular Transport, 26
rue d’Ulm, 75248 Paris Cedex 05, France
Corresponding author: Chavrier, Philippe (philippe.chavrier@curie.fr)
Current Opinion in Cell Biology 2008, 20:454–461
This review comes from a themed issue on
Membranes and organelles
Edited by Graça Raposo and Harald Stenmark
Available online 28th May 2008
0955-0674/$ – see front matter
# 2008 Elsevier Ltd. All rights reserved.
DOI 10.1016/j.ceb.2008.03.011
Introduction
During mitosis of animal cells, an actomyosin-based con-
tractile ring drives the ingression of the cleavage furrow
between the two reforming nuclei, resulting in the for-
mation of a narrow cytoplasmic bridge connecting the two
daughter cells throughout cytokinesis [1]. This bridge is
filled with anti-parallel microtubule bundles interdigitat-
ing in a central electron-dense matrix called the midbody,
and is severed in a process termed abscission representing
the terminal step of cell division.
The mechanism underlying furrow ingression is a long-
standing matter. Many experiments demonstrate the
essential role of actin and myosin II in furrow ingression
[1]. Later, the stability of the intercellular bridge shifts
from an actin-dependent to an actin-independent mode
Current Opinion in Cell Biology 2008, 20:454–461
[2]. Before the actomyosin machinery was even known,
the idea that plasma membrane growth during furrowing
is driven by membrane insertion from some cytoplasmic
membane reservoir was proposed in the late thirties by
A.M. Schechtman who was studying cell division in
salamander Triturus torosus egg [3]. However, a first
description of cytoplasmic vesicles contributing to cell
division came from electron microscopy analysis of maize
root cell division that revealed the accumulation of small
Golgi-derived vesicles, which seemed to coalesce to form
the cell plate [4]. Later studies in Xenopus, zebrafish and
sea urchin embryos also reported that the leading edge of
the ingressing furrow is a site for vesicle insertion [5–8]. In
contrast to eggs or embryonic systems requiring that large
amount of membranes is inserted during furrowing [9], in
other systems including mammalian cells, interfering
with membrane trafficking usually does not prevent
13,14,15,16,17,18]. The existence of membrane
vesicles within the intercellular bridge as been described
by electron microscopy studies for long, but their exact
nature could not be addressed at that time [19]. Depend-
ing of the cell geometry and/or cell types, membrane
transport may thus have distinct contributions at different
moments during cytokinesis.
In this review, we will focus on recent advances in animal
cells concerning the endocytic origin of membranes that
are transported to the intercellular bridge, the character-
ization of the underlying transport mechanisms, and some
– proposed – roles for these membranes during cytokin-
esis. Another important but rarely discussed issue is the
consequences of the very special organization of dividing
cells, which most probably impacts on membrane traf-
ficking during cytokinesis (discussed in Box 1).
Origin of membrane vesicles involved in
cytokinesis
During cytokinesis, Golgi and early recycling/late endo-
somal membranes are clustered at both edges of the
intercellular bridge (see Box 1), and represent potential
reservoirs for vesicles that are trafficked within the inter-
cellular bridge [19,20]. In contrast to plant cells in which
the contribution of the secretory pathway to cytokinesis is
well-established [21], the role of post-Golgi secretory
vesicles to the mechanism of furrowing and abscission
of animal cells remains controversial. Cytokinesis in Cae-
norhabditis elegans and fission yeasts is blocked by Bre-
feldin A (BFA), a drug that inhibits post-Golgi trafficking
[10,22,23]. Yet, the cytokinesis of the first two divisions in
sea urchin egg is insensitive to BFA [8], as for cytokinesis
of Drosophila S2 cells (A.E., unpublished data). In
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 Endocytic traffic in animal cell cytokinesis Montagnac, Echard and Chavrier 455
Box 1 Organelle topology during mitosis
The distribution of intracellular organelles during mitosis is very
specific and reflects the unique organization of the microtubule
network in dividing cells. In interphase both the Golgi complex and
endocytic compartments accumulate at the centrosome in a
microtubule- and dynein-dependent manner (see Figure 1a). During
prophase, the duplicated centrosomes separate and migrate away
from each other and build a bipolar mitotic spindle. At this stage the
Golgi membranes and endosomes are split into two clusters around
each centrosome on both sides of the nucleus [73]. In metaphase,
the characteristic organization of the Golgi apparatus and endoso-
mal compartments undergoes extensive disassembly (Figure 1b)
[74]. At late anaphase and telophase, the cleavage furrow ingresses
and both Golgi and endosomes start to reform and cluster (Figure 1c,
early cytokinesis). In each connected cell, two pools of microtubule
minus-ends are present: one at the centrosome which organizes
distal membrane clusters, and one at the edge of the intercellular
bridge organizing proximal membrane clusters (Figure 1d–e, late
cytokinesis) [17,20,32,73]. The distribution of these membranes in
four separate clusters remains the same until the end of cytokinesis
when proximal Golgi clusters were shown to fuse back with distal
ones on the far side of the nucleus to reconstitute a single Golgi
apparatus in each daughter cell [20]. Although not precisely
described, a similar mechanism for endocytic clusters seems likely.
Central spindle microtubules are thus thought to provide tracks for
polarized transport of membranes from proximal clusters towards
the intercellular bridge.
addition, some studies reported a block of cytokinesis in
human HeLa and A431 cells treated with BFA [14,24],
while others did not observe such effect in rat kidney
NRK cells [25]. Reasons for these discrepancies are not
clear, and may represent differential requirement for
secretory versus endocytic trafficking in the mechanism
of cytokinesis in different cell types as well as differential
sensitivity of both pathways to the drug [26]. In the case of
large embryonic cells, it is also possible that ready-to-fuse
vesicles are already produced during egg maturation
explaining why cytokinesis appears BFA-insensitive.
A somewhat mirrored situation is known for the endocytic
pathway whose contribution to plant cells’ cytokinesis
remains unclear [27,28], while endocytosis from and
recycling to the plasma membrane are clearly essential
for completion of cytokinesis in several animal species
and cell types. Mutations affecting proteins involved in
endocytosis such as clathrin and dynamin lead to cytokin-
esis failure in Dictyostelium amoeba, in C. elegans embryo,
in Drosophila S2 cells and in mammalian cell lines
[2,17,29–31,32,33]. Although clathrin and dynamin
are implicated at different cell locations (not only plasma
membrane, endosomes but also trans-Golgi Network),
proteins of the endocytic machinery at the plasma mem-
brane were shown to be directly required for cytokinesis
[32,33,34]. Analysis of endocytosis in live zebrafish
embryos revealed clathrin coated pits, caveolae and dyna-
min-2 localizing at the cleavage furrow, while inhibitors of
endocytosis prevented completion of cytokinesis [35].
One possible function for endocytosis during cytokinesis
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maybe the recycling of components of the cleavage
furrow.
In mammalian cells, several studies concluded that re-
ceptor-mediated endocytosis, including transferrin
uptake, is shut down during early mitosis [36,37]. How-
ever, it has recently been shown that receptor-mediated
endocytosis of transferrin resumes during cytokinesis and
differentially occurs at the poles or closed to the inter-
cellular bridge during early and late cytokinesis, respect-
ively [32]. In addition, another recent report showed that
the rate of endocytosis (measured by uptake of a fluid-
phase marker) does not decrease during mitosis, but
rather the amount of surface receptors (including the
transferrin-receptor) decreases, owing to a block of recy-
cling and to receptors remaining trapped within the
mitotic cell [17]. Unbalanced endocytic/recycling rates
would explain the reduction in cell surface area accom-
panying the onset of mitosis and cell rounding. Then,
recycling resumes at telophase, allowing daughter cells’
plasma membrane to regrow during cytokinesis [17].
Mitotic cell blebbing, which correlate with membrane
recycling and insertion during plasma membrane
regrowth, was shown to be independent of the secretory
pathway, and to require the activity of vesicle-associated
membrane protein (VAMP)-3 and VAMP-7, two endocy-
tic vesicular-soluble N-ethylmaleimide-sensitive factor
attachment protein receptors (v-SNAREs) implicated
in exocytic fusion events of early recycling and late
endocytic compartments with the plasma membrane,
respectively [17]. Interestingly, there is a spatial control
of endocytic internalization and recycling during cytokin-
esis. In particular, receptor-mediated internalization
occurs at the plasma membrane in the polar regions
during late anaphase, and internalized material is recycled
preferentially towards the intercellular bridge region
[32]. In addition, analysis of GFP-clathrin revealed a
complex pattern of endocytic internalization in the furrow
and bridge regions [38]. Thus, endocytosis and recycling
must be tightly regulated in both a spatial and temporal
fashion during mitosis exit, by mechanisms that remain to
be elucidated.
Targeting of recycling membranes to the
midbody
It has become evident over the past few years that
polarized recycling of internalized membranes toward
the bridge is important for abscission [39,40]. The first
functional implication of membrane recycling during
cytokinesis came from RNA interference of Rab11 in
C. elegans embryos [10]. In interphase cells, the small
GTP-binding protein Rab11 localizes to recycling endo-
somes (REs) where it is mainly required for the recycling
of vesicles from RE to the plasma membrane, although
some role in RE-to-Golgi/TGN transport has also been
proposed [41,42]. Rab11 depletion by RNAi in human
HeLa cells and Drosophila S2 cells confirmed the implica-
Current Opinion in Cell Biology 2008, 20:454–461
456 Membranes and organelles

Figure 1

Organelle topology during mitosis and cytokinesis. (a–d) As described in Box 1, the Golgi apparatus and recycling endocytic compartments
undergo an extensive reorganisation during mitosis and cytokinesis related to the specialized organization of microtubule network (minus ( ) and
plus (+) ends of microtubules are indicated). Membrane clusters referred as proximal (p) and distal (d) to the intercellular bridge are indicated. (e) HeLa
cells at late telophase/cytokinesis exhibit four clusters of Golgi vesicles labeled with giantin (pseudocolored red) and transferrin-positive endosomes
(green) positioned proximally and distally to the intercellular bridge. Microtubules stained for a-tubulin are visible in blue. Scale bar, 5 mm.

tion of Rab11 in cytokinesis, but the exact contribution of
Rab11 in bridge stability versus abscission remains to be
quantitatively investigated [16,43]. Consistent with a
role of this GTPase in late cytokinesis events, Rab11
accumulates at the intercellular bridge in mammalian
cells [44,45]. Together, these data emphasize the require-
ment for endocytic recycling in post-furrowing cytokin-
esis events.
In parallel, an increasing number of Rab11-interacting
proteins have been implicated in cytokinesis. In particu-
lar, Rab11 family interacting protein-3 (FIP3) and the
related FIP4 protein, were identified as downstream
effectors of Rab11 on REs and have two main localiz-
ations at both proximal and distal RE clusters (Box 1) and
at the intercellular bridge in mammalian cells [44–47].
While FIP3/4 association with RE clusters is clearly
Rab11-dependent, its bridge localization is not (see
Box 1, [44,45,48]). Interfering with Rab11 or FIP3/4
function, or with Rab11:FIP interaction was shown to
affect abscission, while having no effect on furrowing
[45]. The fact that a fraction of cells become binucleated
indicates also a contribution of those proteins in the
intercellular bridge stability.
FIP3/4 were also named arfophilin1/2 on the basis of their
ability to interact with small GTP-binding proteins of the
ADP-ribosylation factor (ARF) subgroup including

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 Endocytic traffic in animal cell cytokinesis Montagnac, Echard and Chavrier 457

ARF6, a protein known to regulate early endocytic recy-
cling [48,49–51]. ARF6 becomes activated during cyto-
kinesis in HeLa cells and a GTP-bound (activated)
mutant of ARF6 localizes at the midbody during cytokin-
esis [48,52]. Importantly, ARF6 controls the recruitment
of FIP3/4 to the intercellular bridge and is involved for
abscission. Binding sites for Rab11 and ARF6 that are
found at the C-terminus of FIP3/4 are spatially distinct,
allowing the formation of ternary complexes, with FIP3/4
possibly acting as a bridge between ARF6 and Rab11
[48,51].
In addition, recruitment of FIP3/4 and Rab11 to the
midbody involves the exocyst complex [48]. This octa-
meric complex, which controls the docking of exocytic
vesicles to the plasma membrane [53], is a common
partner of Rab11 (interacting with Sec15) and ARF6
(through Sec10) [54,55]. Exocyst components localize
to the midbody and are essential for completion of cyto-
kinesis [2,14,34,48]. Together these data suggest a
scenario in which Rab11, ARF6 and their common effec-
tors FIP3/4 and exocyst work in concert during cytokin-
esis in a mechanism whereby ARF6 controls the
recruitment and docking of Rab11-positive recycling
endocytic vesicles to the midbody (see Figure 2). Regu-
lation of exocyst-dependent RE trafficking during cyto-
kinesis may also involve RalA, a small GTP-binding
proteins that is known to interact with Exo84 and Sec5
exocyst components [15].
Interestingly, analysis of ARF6 and Rab11 mutants in
Drosophila recently demonstrated that these two proteins
are required for meiotic cytokinesis in spermatocytes.
Although most Rab11 mutations in Drosophila are lethal,
less penetrant semi-lethal Rab11 mutations have been
found and result in male sterility correlated with the
presence of multinucleated spermatids [56]. Similarly,
arf6 null mutation, although not lethal, also resulted in a
majority of spermatids with two or four nuclei [18]. In
arf6 mutants, the cleavage furrow was found to regress
because of a failure in rapid endocytic membrane addition
to the plasma membrane [18]. Rab11 accumulates at the
cleavage furrow of Drosophila spermatocytes, and has
been shown to be required for cleavage furrow ingression
[56]. On the basis of abnormal accumulation of Golgi-
derived vesicles within the bridge that failed to constrict,
the authors proposed that Rab11 mediates Golgi mem-
brane addition at the furrow [56]. However, Nuf, the
Drosophila FIP3/4 homolog, was mislocalized in Rab11
mutants, suggesting also some possible defects of RE

Figure 2

Model for membrane trafficking at cytokinesis. Activated GTP-bound Rab11 interacts with and recruits FIP3/FIP4 scaffolding proteins and the
exocyst complex (via Sec15 subunit of the exocyst complex) to vesicles originating from a cluster of recycling endosomes proximal to the intercellular
bridge. These vesicles move within the intercellular bridge towards the plus-ends of central spindle microtubules via interaction with a plus-end
directed motor, possibly kinesin-1. Minus-end directed dynein may control movement out of the intercellular bridge. At the midbody, ternary
interactions of Rab11/FIP and Rab11/exocyst with GTP-bound ARF6 mediate the anchoring and docking of the vesicles to the plasma membrane.
Pairing of v/t-SNAREs may trigger the homotypic coalescence of vesicles in larger membrane structures that accumulate at the midbody and their
heterotypic fusion with the plasma membrane in a mechanism required for abscission. Rab35 is found at the plasma membrane and on
endocytic vesicles, and regulates a fast endocytic recycling pathway required for PIP2 enrichment at the intercellular bridge and cytokinesis.
Minus ( ) and plus (+) ends of microtubules are indicated.

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458 Membranes and organelles
trafficking during meiotic cytokinesis. Whether Rab11’s
predominant function in post-Golgi trafficking is specific
to Drosophila spermatocytes is presently unknown. An
important question will be also to understand why
reduction of ARF6 or Rab11 functions affects cytokinesis
essentially in spermatocytes. One possibility is that
Rab11 and ARF6 could have partially redundant func-
tions, as suggested recently in mammalian cells [43]. In
any case, these data reinforce the view that Rab11 and
ARF6 are key players for regulating membrane trafficking
during cytokinesis. Besides Rab11 and ARF6, a systema-
tic RNAi-based screen for Rab proteins involved in
cytokinesis in Drosophila S2 cells identified Rab35,
another Rab protein involved in membrane recycling
[16] (see below), which appears not to be connected
to the Rab11 pathway (Figure 2; A.E., unpublished data).
Finally, on the basis of the expression of dominant
inhibitory mutant forms, SNARE proteins have also been
shown to be required for successful cytokinesis in med-
iating terminal events following delivery and anchoring of
vesicles at the midbody. Beside several secretory
SNARE-family members that are essential during cyto-
kinesis [39,40], endocytic SNAREs are also involved for
completion of abscission. As mentioned earlier, VAMP-3
and VAMP-7 have been found to control unpolarized
exocytosis of REs and late endosomes, respectively,
underlying the process of blebbing that occurs during
plasma membrane growth at cytokinesis [17]. In
addition, endocytic v-SNAREs, VAMP-8 and VAMP-2
and their cognate target (t)-SNAREs, syntaxin-2 and
synaptosomal-associated protein 25 (SNAP-25), respect-
ively, are recruited to the cleavage furrow and to the
midbody [12,57]. However, VAMP-8/syntaxin-2 and
VAMP-2/SNAP-25 do not appear to contribute signifi-
cantly to furrow invagination, and are rather essential at
terminal steps of cytokinesis during abscission in mam-
malian cells and apposition of blastomers in early zebra-
fish embryos, respectively [12,57]. Interestingly, exocyst
depletion results in accumulation of VAMP-8 positive
endocytic vesicles [14]. Noticeably, the exocyst com-
plex, beside its function in post-Golgi trafficking, is also
localized to endocytic recycling compartments where it
controls membrane recycling to the plasma membrane
[55]. Moreover trafficking of secretory cargoes to the
plasma membrane through endocytic recycling compart-
ments have been reported in a mechanism implicating
the exocyst complex [58]. Together, these data suggest
the possibility that convergence between secretory and
endocytic pathways is required for cytokinesis.
Open matters
Role of membrane addition in late steps of cytokinesis
Advances in the past few years clearly led to the idea that
membrane traffic plays a critical role in the late stages of
cytokinesis in animal cells, as previously demonstrated in
plant cells [21]. As the molecular intracellular traffic
Current Opinion in Cell Biology 2008, 20:454–461
machineries are being identified, an important question
is to decipher the exact roles of secretion and endocytosis
in cytokinesis. Reminiscent of plant phragmoplast
vesicles which fuse and coalesce into large units of
membrane, vesicles generated by trafficking from RE
and from the Golgi that accumulate in the midbody
may undergo homotypic fusion events resulting in abscis-
sion in animal cells [14]. Of note the attractive parallel
in terminal events of cytokinesis in plant and animal cells
must only be partial, as superior plant cells are connected
one to each other by plasmodesmata and no abscission
occurs as cell proliferate. In animal cells, it was recently
reported that secretory vesicles (possibly connected to
endocytic recycling pathways, as discussed above)
accumulate at the intercellular bridge, followed by their
sudden disappearance before abscission occurs [14]. It is
now crucial to understand by which mechanisms homo-
typic fusion (between vesicles themselves) and hetero-
typic fusion (between vesicles and the plasma membrane)
can be coordinated and lead to the physical abscission of
the intercellular bridge (see Figure 2). Another key
question is to determine where exactly within the inter-
cellular bridge the abscission occurs (we know that it is
asymmetric as only one of the two daughter cells inherits a
bridge remnant) and how microtubules of the bridge do
not physically prevent this process. Abscission is also
likely assisted by a progressive diminution of the
diameter of the intercellular bridge associated with a
specific curvature [19]. An intriguing, yet poorly under-
stood observation is that proteins of the endosomal sorting
complex required for transport (ESCRT) complexes and
ESCRT interacting protein ALIX, which function at late
endosomes to sort membrane proteins into the lumen to
create multivesicular bodies, interact with protein of the
midbody such as CEP55 and are required for cytokinesis
[59–61]. Whether the ESCRT machinery contributes to
some trafficking of late endocytic structures to the bridge,
or whether it performs some other functions required for
severing the bridge is presently unknown. Recent struc-
tural data about ESCRT proteins however suggest that
these complexes are able to induce membrane defor-
mations that could be important for cytokinesis and other
topologically related process such as retrovirus budding or
inward vesicle budding in late endocytic compartments
[62]. Finally, membrane addition could have a greater
qualitative than quantitative importance during the term-
inal steps of cytokinesis by targeting specific cargoes
essential for abscission. This has been recently suggested
for phosphorylated proteins that are transported in the
intercellular bridge in a Rab11-dependent manner [63].
Role of lipid domains at the intercellular bridge during
cytokinesis
Dynamic changes in membrane lipid composition during
furrowing and at the midbody are essential for completion
of cytokinesis. Phosphoinositide kinases and their pro-
ducts phosphatidylinositol polyphosphates, in particular
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 Endocytic traffic in animal cell cytokinesis Montagnac, Echard and Chavrier 459
phosphatidylinositol (4,5) bisphosphate (PIP2) is pro-
duced and enriched at the furrow and it is required for
cytokinesis in different species [64–66]. Cytokinesis
defects in rab11 or arf6 mutant Drosophila spermatocytes
are reminiscent of the ‘four-wheel-drive’ ( fwd) pheno-
type that is caused by loss of phosphatidylinositol 4-
kinase activity, an enzyme implicated in the generation
of PIP2 [18,56,67]. Consistently, ARF6 is known to
control the production of PIP2 through the regulation
of phosphatidylinositol 4-phosphate 5-kinase alpha in
animal cells [50,68]. In addition, Rab35 was recently
identified as a Rab protein regulating fast endocytic
recycling that contributes to proper localization and main-
tenance of PIP2 at the intercellular bridge during cyto-
kinesis in animal cells [16]. Yet, potential ligands of
membrane PIP2 possibly involved in cytokinesis are
numerous, including proteins involved in actin dynamics,
regulators of small GTP-binding proteins and members of
the septin family. As functional inactivation of Rab35 and
SEPTIN2 result in similar post-furrowing defects and
that Rab35 is required for SEPTIN2 enrichment at the
intercellular bridge, a proposed function for Rab35 is to
regulate PIP2 and thus proper septin localization during
cytokinesis [16]. Other lipid domains, including choles-
terol-rich domains, are enriched at the furrow/intercellu-
lar bridge by unknown mechanisms, and also appear
important for post-furrowing cytokinesis events [69].
Together, these data highlight the importance of mem-
brane compartmentalization into subdomains for abscis-
sion that may restrict signalling events, vesicle anchoring
and fusion events at the appropriate site and time within
the bridge.
Significance and regulation of bidirectionnal membrane
traffic within the intercellular bridge
Finally and despite a large body of work implicating
polarized membrane delivery towards the bridge as a
key mechanism for abscission, molecular motors involved
in moving this membrane material remain poorly charac-
terized. It is likely that MT bundles of the central spindle
provide tracks to facilitate vesicle movement. A plus-end
directed motor, KIF3B (kinesin-2), transports Golgi-
associated spectrin syne-1 to the bridge [70]. In addition,
a proteomic dissection of the midbody demonstrated that
conventional kinesin (kinesin-1) is indeed present at the
midbody making it another attractive candidate for mov-
ing membranes from the edges to the center of the
midbody [34]. Unpublished data demonstrate that kine-
sin-1 is essential for moving membranes from proximal
RE clusters into the intercellular bridge (R. Prekeris,
personal communication; G.M. and P.C., unpublished).
Conversely, components of the dynactin complex regu-
lating the activity of the minus-end dynein motor are also
required for cytokinesis ([71], G.M. and P.C., unpub-
lished). Finally, myosin VI, a member of the myosin-
family of actin-dependent motors was recently implicated
in the movement of vesicles into the bridge [72].
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Together, these observations suggest that complex bi-
directional movements of vesicles are important for the
mechanism of abscission. Dynamic remodelling of lipid/
protein composition may be the reason for such bidirec-
tional transport requirement, and further studies should
clarify this important issue.
Acknowledgements
We apologize to those colleagues whose work could not be discussed
because of space limitations. Work in P.C.’s laboratory is funded by the
CNRS, the Institut Curie, La Fondation BNP-Paribas and La Ligue
Nationale contre le Cancer (‘‘équipe labellisée’’). G.M. is a recipient of a
postdoctoral fellowship from Association pour la Recherche sur le Cancer.
Work in A.E. group is supported by the Association pour la Recherche sur le
Cancer and the ANR (grant JC07-188506).
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