Endocytosis

Endocytosis is a cellular process in

which substances are brought into the
cell. The material to be internalized is
surrounded by an area of cell
membrane, which then buds off inside
the cell to form a vesicle containing the
ingested material. Endocytosis
includes pinocytosis (cell drinking)
and phagocytosis (cell eating). It is a
form of active transport.

The different types of endocytosis

Contents
History
Pathways
Principal components
Clathrin-mediated
Processes and components
Mechanisms
Gallery
See also
References
Further reading
External links

History
The term was proposed by De Duve in 1963.[1] Phagocytosis was discovered by Élie Metchnikoff in
1882.[2]

Pathways
Endocytosis pathways can be subdivided into four categories: namely, receptor-mediated endocytosis (also
known as clathrin-mediated endocytosis), caveolae, pinocytosis, and phagocytosis.[3]
Clathrin-mediated endocytosis is mediated by the
production of small (approx. 100 nm in diameter)
vesicles that have a morphologically characteristic coat
made up of the cytosolic protein clathrin.McMahon HT,
Boucrot E (July 2011). "Molecular mechanism and
physiological functions of clathrin-mediated
endocytosis". Nature Reviews. Molecular Cell Biology.
12 (8): 517–33. doi:10.1038/nrm3151 (https://doi.org/10.1
038%2Fnrm3151). PMID 21779028 (https://pubmed.ncb
Schematic drawing illustrating
i.nlm.nih.gov/21779028). S2CID 15235357 (https://api.se
clathrin-mediated (left) and clathrin-
manticscholar.org/CorpusID:15235357). Clathrin-coated
independent endocytosis (right) of
vesicles (CCVs) are found in virtually all cells and form
synaptic vesicle membranes.
domains of the plasma membrane termed clathrin-
coated pits. Coated pits can concentrate large
extracellular molecules that have different receptors
responsible for the receptor-mediated endocytosis of ligands, e.g. low density lipoprotein,
transferrin, growth factors, antibodies and many others.[4]

Study [5] in mammalian cells confirm a reduction in clathrin coat size in an increased
tension environment. In addition, it suggests that the two apparently distinct clathrin
assembly modes, namely coated pits and coated plaques, observed in experimental
investigations might be a consequence of varied tensions in the plasma membrane.

Caveolae are the most commonly reported non-clathrin-coated plasma membrane buds,
which exist on the surface of many, but not all cell types. They consist of the cholesterol-
binding protein caveolin (Vip21) with a bilayer enriched in cholesterol and glycolipids.
Caveolae are small (approx. 50 nm in diameter) flask-shape pits in the membrane that
resemble the shape of a cave (hence the name caveolae). They can constitute up to a third
of the plasma membrane area of the cells of some tissues, being especially abundant in
smooth muscle, type I pneumocytes, fibroblasts, adipocytes, and endothelial cells.[6] Uptake
of extracellular molecules is also believed to be specifically mediated via receptors in
caveolae.
Potocytosis is a form of
receptor-mediated
endocytosis that uses
caveolae vesicles to bring
molecules of various sizes
into the cell. Unlike most
endocytosis that uses
caveolae to deliver contents
of vesicles to lysosomes or
other organelles, material
endocytosed via potocytosis
is released into the cytosol.[7] From left to right: Phagocytosis, Pinocytosis, Receptor-mediated
Pinocytosis, which usually endocytosis.
occurs from highly ruffled regions
of the plasma membrane, is the
invagination of the cell membrane to form a pocket, which then pinches off into the cell to
form a vesicle (0.5–5 µm in diameter) filled with a large volume of extracellular fluid and
molecules within it (equivalent to ~100 CCVs). The filling of the pocket occurs in a non-
specific manner. The vesicle then travels into the cytosol and fuses with other vesicles such
as endosomes and lysosomes.[8]
 Phagocytosis is the process by which cells bind and internalize particulate matter larger
than around 0.75 µm in diameter, such as small-sized dust particles, cell debris,
microorganisms and apoptotic cells. These processes involve the uptake of larger
membrane areas than clathrin-mediated endocytosis and caveolae pathway.

More recent experiments have suggested that these morphological descriptions of endocytic events may be
inadequate, and a more appropriate method of classification may be based upon whether particular
pathways are dependent on clathrin and dynamin.

Dynamin-dependent clathrin-independent pathways include FEME, UFE, ADBE, EGFR-NCE and IL2Rβ
uptake.[9]

Dynamin-independent clathrin-independent pathways include the CLIC/GEEC pathway (regulated by

Graf1),[10] as well as MEND and macropinocytosis.[9]

Clathrin-mediated endocytosis is the only pathway dependent on both clathrin and dynamin.

Principal components
The endocytic pathway of mammalian cells consists of distinct membrane compartments, which internalize
molecules from the plasma membrane and recycle them back to the surface (as in early endosomes and
recycling endosomes), or sort them to degradation (as in late endosomes and lysosomes). The principal
components of the endocytic pathway are:[3]

Early endosomes are the first compartment of the endocytic pathway. Early endosomes are
often located in the periphery of the cell, and receive most types of vesicles coming from the
cell surface. They have a characteristic tubulo-vesicular structure (vesicles up to 1 µm in
diameter with connected tubules of approx. 50 nm diameter) and a mildly acidic pH. They
are principally sorting organelles where many endocytosed ligands dissociate from their
receptors in the acid pH of the compartment, and from which many of the receptors recycle to
the cell surface (via tubules).[11][12] It is also the site of sorting into transcytotic pathway to
later compartments (like late endosomes or lysosomes) via transvesicular compartments
(like multivesicular bodies (MVB) or endosomal carrier vesicles (ECVs)).
Late endosomes receive endocytosed material en route to lysosomes, usually from early
endosomes in the endocytic pathway, from trans-Golgi network (TGN) in the biosynthetic
pathway, and from phagosomes in the phagocytic pathway.[13] Late endosomes often
contain proteins characteristic of nucleosomes, mitochondria and mRNAs including
lysosomal membrane glycoproteins and acid hydrolases. They are acidic (approx. pH 5.5),
and are part of the trafficking pathway of mannose-6-phosphate receptors. Late endosomes
are thought to mediate a final set of sorting events prior the delivery of material to lysosomes.
Lysosomes are the last compartment of the endocytic pathway. Their chief function is to
break down cellular waste products, fats, carbohydrates, proteins, and other
macromolecules into simple compounds. These are then returned to the cytoplasm as new
cell-building materials. To accomplish this, lysosomes use some 40 different types of
hydrolytic enzymes, all of which are manufactured in the endoplasmic reticulum, modified in
the Golgi apparatus and function in an acidic environment.[14] The approximate pH of a
lysosome is 4.8 and by electron microscopy (EM) usually appear as large vacuoles (1-2 µm
in diameter) containing electron dense material. They have a high content of lysosomal
membrane proteins and active lysosomal hydrolases, but no mannose-6-phosphate
receptor. They are generally regarded as the principal hydrolytic compartment of the
cell.[15][16]

It was recently found that an eisosome serves as a portal of endocytosis in yeast.[17]

Clathrin-mediated
The major route for endocytosis in most cells, and the best-understood, is that mediated by the molecule
clathrin.[18][19] This large protein assists in the formation of a coated pit on the inner surface of the plasma
membrane of the cell. This pit then buds into the cell to form a coated vesicle in the cytoplasm of the cell. In
so doing, it brings into the cell not only a small area of the surface of the cell but also a small volume of
fluid from outside the cell.[20][21][22]

Coats function to deform the donor membrane to produce a vesicle, and they also function in the selection
of the vesicle cargo. Coat complexes that have been well characterized so far include coat protein-I (COP-
I), COP-II, and clathrin.[23][24] Clathrin coats are involved in two crucial transport steps: (i) receptor-
mediated and fluid-phase endocytosis from the plasma membrane to early endosome and (ii) transport from
the TGN to endosomes. In endocytosis, the clathrin coat is assembled on the cytoplasmic face of the plasma
membrane, forming pits that invaginate to pinch off (scission) and become free CCVs. In cultured cells, the
assembly of a CCV takes ~ 1min, and several hundred to a thousand or more can form every minute.[25]
The main scaffold component of clathrin coat is the 190-kD protein called clathrin heavy chain (CHC),
which is associated with a 25- kD protein called clathrin light chain (CLC), forming three-legged trimers
called triskelions.

Vesicles selectively concentrate and exclude certain proteins during formation and are not representative of
the membrane as a whole. AP2 adaptors are multisubunit complexes that perform this function at the
plasma membrane. The best-understood receptors that are found concentrated in coated vesicles of
mammalian cells are the LDL receptor (which removes LDL from circulating blood), the transferrin
receptor (which brings ferric ions bound by transferrin into the cell) and certain hormone receptors (such as
that for EGF).

At any one moment, about 25% of the plasma membrane of a fibroblast is made up of coated pits. As a
coated pit has a life of about a minute before it buds into the cell, a fibroblast takes up its surface by this
route about once every 16 minutes. Coated vesicles formed from the plasma membrane have a diameter of
about 36 nm and a lifetime measured in a few seconds. Once the coat has been shed, the remaining vesicle
fuses with endosomes and proceeds down the endocytic pathway. The actual budding-in process, whereby
a pit is converted to a vesicle, is carried out by clathrin assisted by a set of cytoplasmic proteins, which
includes dynamin and adaptors such as adaptin.

Coated pits and vesicles were first seen in thin sections of tissue in the electron microscope by Matt Lions
and Parker George. The importance of them for the clearance of LDL from blood was discovered by
Richard G. Anderson, Michael S. Brown and Joseph L. Goldstein in 1977.[26] Coated vesicles were first
purified by Barbara Pearse, who discovered the clathrin coat molecule in 1976.[27]

Processes and components

Caveolin proteins like caveolin-1 (CAV1), caveolin-2 (CAV2), and caveolin-3 (CAV3), play significant
roles in the caveolar formation process. More specifically, CAV1 and CAV2 are responsible for caveolae
formation in non-muscle cells while CAV3 functions in muscle cells. The process starts with CAV1 being
synthesized in the ER where it forms detergent-resistant oligomers. Then, these oligomers travel through
the Golgi complex before arriving at the cell surface to aid in caveolar formation. Caveolae formation is
also reversible through disassembly under certain conditions such as increased plasma membrane tension.
These certain conditions then depend on the type of tissues that are expressing the caveolar function. For
example, not all tissues that have caveolar proteins have a caveolar structure ie. the blood-brain barrier.[28]
Though there are many morphological features conserved among caveolae, the functions of each CAV
protein are diverse. One common feature among caveolins is their hydrophobic stretches of potential
hairpin structures that are made of α-helices. The insertion of these hairpin-like α-helices forms a caveolae
coat which leads to membrane curvature. In addition to insertion, caveolins are also capable of
oligomerization which further plays a role in membrane curvature. Recent studies have also discovered that
polymerase I, transcript release factor, and serum deprivation protein response also play a role in the
assembly of caveolae. Besides caveolae assembly, researchers have also discovered that CAV1 proteins can
also influence other endocytic pathways. When CAV1 binds to Cdc42, CAV1 inactivates it and regulates
Cdc42 activity during membrane trafficking events.[29]

Mechanisms

The process of cell uptake depends on the tilt and chirality of constituent molecules to induce membrane
budding. Since such chiral and tilted lipid molecules are likely to be in a "raft" form, researchers suggest
that caveolae formation also follows this mechanism since caveolae are also enriched in raft constituents.
When caveolin proteins bind to the inner leaflet via cholesterol, the membrane starts to bend, leading to
spontaneous curvature. This effect is due to the force distribution generated when the caveolin oligomer
binds to the membrane. The force distribution then alters the tension of the membrane which leads to
budding and eventually vesicle formation.[30]

Gallery
Endocytosis. For example, coronavirus SARS-CoV-2 binds to the ACE2 receptor of the
epithelial cell.

Stage 1 Stage 2

0:00

Stage 3 Endocytosis animation (1)

 0:00

Endocytosis animation (2)

See also
Active transport
Emperipolesis
RAP6 (Rab5-activating protein 6)
Exocytosis
Phagocytosis
Pinocytosis
Trans-endocytosis

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Further reading
Doherty GJ, McMahon HT (2009). "Mechanisms of endocytosis". Annual Review of
Biochemistry. 78: 857–902. doi:10.1146/annurev.biochem.78.081307.110540 (https://doi.or
g/10.1146%2Fannurev.biochem.78.081307.110540). PMID 19317650 (https://pubmed.ncbi.
nlm.nih.gov/19317650).

External links
Endocytosis at biologyreference.com (http://www.biologyreference.com/Dn-Ep/Endocytosis.
html)
Endocytosis - researching endocytic mechanisms at endocytosis.org (http://www.endocytosi
s.org)
Clathrin-mediated endocytosis (http://www.cellimagelibrary.org/images/12257) ASCB Image
& Video Library
Types of Endocytosis (Animation) (http://highered.mcgraw-hill.com/olc/dl/120068/bio02.swf)

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