1.

Membrane Structure and Function

2. Trans-Membrane Transport
3. Endocytosis

Cytoskeleton: microfilaments, microtubules, Intermediate filaments

4. Microfilaments – globular monomers of G-actin polymerize to form helical filaments of F-actin;

ATP dependent polymerization
a. Actin
i. Structure:
1. F-actin helical filaments composed of globular monomers of G-actin
(polymerization is ATP dependent)
2. Constantly undergoing assembly and disassembly (+ end polymerizes
while – end depolymerizes) – “Treadmilling” balance of activity
3. Distinct polarity;
4. Depending on other proteins, actin filaments can be spaced out (lung)
or close together (muscle)
ii. Functions: In conjunction with myosin, actin microfilaments provide contractile
and motile forces of cells
1. Muscle contraction
a. Dystrophin is intermediate protein that anchors actin to trans-
membrane protein, which is anchored to the extra-cellular
matrix, and is required for muscle to contract;
b. Without dystrophin – disorganized contraction leads to death
from inability to contract diaphragm to breath
2. Cell locomotion
a. Involves integrin
3. Cytokinesis – actin filaments form the contractile ring that is the basis of
cytokinesis during mitosis and meiosis
4. Actin anchors TM proteins (via intermediary proteins specific to a
Transmembrane protein); serves to localize to a particular area – e.g.
receptors to a synapse, desmosome, gap junctions)
a. Link to cell membranes at tight junctions and at zonula
adherens
5. Organelle movement due to Actin Anchoring
6. Forms nets – filamin brings actin together at 90 degress; ARP enables 70
degree branching angles – the only component of the cytoskeleton that
can do this
7. Maintain cell shape
a. Mediate platelet shape change (i.e. clotting); initially actin is
capped and cannot grow, calcium influx activates a protein
which cuts actin into smaller pieces, allowing it to polymerize
8. Anchor microvilli – form the core of microvilli
9. Act as a railroad track – myosin head affinity for actin, myosin tail binds
other things in the cell and moves them along the actin track
 10. Phagocytosis (actin polymerizes so plasma membrane wraps around a
bacteria
11. Yeast budding requires actin – ARP is activated -> actin polymerizes,
changes shape
12. Microtubule anchor in cilia and flagella
5. Microtubules
a. Structure
i. Microtubules has cylindrical outer structure composed of a helical arrary of
polymerized heterodimers of alpha and beta tubulin; each dimer bound by two
GTP
1. Incorporated in flagella, cilia, mitotic spindles
ii. Microtubules grow slowly and collapse quickly (grow from the + end); similar to
actin, undergo continuous assembly and disassembly
1. Polymerize starting at an MTOC where – end is attached;
a. + end points to the periphery
b. – end near nucleus
iii. Cilia: 9 doublets + 2 singlet arrangement of microtubules
1. Basal body (base of a cilium below the cell membrane) of 9 microtubule
triplets with no central microtubules
b. Function: provide tracks for intra-cellular transport of vesicles and molecules
i. Cilia and flagella (9 peripheral doublets and 1 central doublet – connected with
axonemal dynein, ATPase movement links 9 peripheral doublets and cause
bending of cilia by differential sliding of doublets)
1. In protozoa, lung epithelium cilia, fallopian tube cilia, sperm flagella,
Chlamydomonas (2 flagella), single cilia per cell in embryo propels cells
along concentration gradients
ii. Muscle contraction is triggered by calcium influx whereas flow of liquid bends
cilia which cause calcium to enter, then influences other cells cilia to beat
iii. Involved in slow axoplasmic transport in neurons
iv. Transport cellular cargo/organelles towards opposite end of tracks with Dynein
and Kinesin (D & K both have head w affinity for MT and tail with adapter
protein that is cargo specific); transport requires specific ATPase motor
molecules
1. Dynein(retrograde) move + to –
2. Kinesin (anterograde) moves – to +
v.
c. Ciliated cells:
i. Fallopian tubes (destruction by Chlamydia leads to infertility)
ii. Respiratory Epithelium (smoking destroys cilia)
iii. Tympanus of ear for hearing (mechanically sensitive calcium channels
d. Mictrotubule Organizing Center (MTOC)
i. Organization of actin and microtubules (in the MTOC) are involved in sealing an
immunological syncapse between a T cell and its target so that preotease action
is contained
 ii. MTOC is made of 2 perpendicular tubes and is found in every cell
iii. Centrioles are MTOCs which anchor the spindle during mitosis (each cell has
one, two while dividing)
iv. MTOC has a gamma tubulin (in addition to the usual alpha and beta tubulin that
makes up microtubules) and 9 peripheral triplets, NO central cylinder
v. MTOC is like a basal body for cilia and flagella
1. Cilia is 9 doublets + 2 in the middle; the base of cilium below the cell
membrane is 9 microtubule triplets
2. Axonemal
vi. MTOC divides without DNA – one serves as the template for another
e. Microtubule inhibition
i. Taxol: inhibits MT DISASSEMBLY causing clumping of microtubules and cell
death
1. Found in nature but produced synthetically
2. Effective, extremely toxic
ii. Vincristine & Vinblastine: prevent MT polymerization
1. Come from Vinca plants; were early anti-cancer drugs
2. Primarily used against Leukemia
3. Note: drugs can’t be used against actin for cancer treatment because it
is too toxic, causing cell death
6. Intermediate Filaments
a. Structure: 10 nm diameter filaments that are usually stable once formed
i. 30 different possible monomers
ii. Form doublets > plane > fold > strong fibers
iii. Have a homologous area, but monomers different at N and C terminals in tissue
specific way (this helps pathologist ID cell’s tissue of origin after metastases
1. Lamins are monomer of IF in the nucleus; support nucleus from the
inside (please laminate my nucleus, its important)
2. Keratin found in epithelial layers (hair, hooves, horns) – keratin
mutation weakens cell-cell conections, leading to easy blistering and
easy infection
b. Function: Stabilize and strengthen (not involved in movement like MTs and MFs)
c. 4 Types:
i. Type I – Keratins – found in all epithelial cells
ii. Type II – Diverse group;
1. Desmin – found in skeletal, cardiac, GI tract smooth muscle cells
2. Vimentin – found in fibroblasts, fibrocytes, endothelial cells, vascular
smooth muscle
3. Glial fibriallary acidic protein in astrocytes and some Schwann cells
4. Peripherin found in peripheral nerve axons
iii. Type III: neurofilaments in neurons
iv. Type IV: 3 types of lamins forming a meshwork rather than individual cilaments
inside the nuclear envelope of all cells
d. Disease Process: ALS
 i. Motor neurons die due to an accumulation of Ifs

7. Random attachment of MTs to chromosomes during mitosis

a. Chromosome pairing is specific
8. Microfilaments and Intermediate filaments both support + attach to transmembrane proteins
which form structures that connect to other cells and the ECM. Microfilaments and
Intermediate Filaments
9. Organelle duplication:
a. Nucleus – lamins are phosphorylated and disassemble while still attached to nuclear
membrane; multiple vesicles of nuclear membrane w free lamins > some vesicles end up
in each daughter cell > mini nuclear membrane around each single chromosome > fuse >
Intermediate filaments rebuild/stabilize
10. Physical Properties of 3 cytoskeletal elements
a. Microfilaments/Actin – like steel – hard to bend, strong, will break
b. Intermediate Filaments – easy to deform, but don’t really break – strong, make up the
main structural net of cells so have to be deformable but at same time strong, nearly
unbreakable
c. Microtubules – easy to bend, will break at some point; cytoskeletal elements are always
moving around

11. Protein Sorting: Endoplasmic Reticulum and Golgi Apparatus

12. Mitochondira
13. Protein Degradation: Ubiquitin
14. Biology of Cancer