anchoring

transport

main difference:
- size, function

actin!!!!!

during contraction I bands shorten!!! VERY HIGH YEILD

muscle contraction
-voluntary
-mutlinucleated
-nucleus in periphery

globular actin becomes filamentous

actin due to ATP

binds calcium
inhibitory

cells dont shorten right away because

they are capped

binds tropomyosin
hinders the power stroke

DHSR - receptor is high yeild

caps actin at the negative end-keeps it from depolymerizing

caps actin on plus end to z disc
holds filaments of actin in between z -discs
binds myosin to z-disc
only has one heavy chain

binds actin negative end to z-disk

binds mysoin to m-line

ventricular transport

know these steps!!! HIGH YEILD

confirmation change
jump and rebind actin

calcium pump - primary active transport

adhere cells together

cardiac muscle are connected via discs,
these discs have three componenets

special nerve cells that carry signals from

SA node to AV node to the ventircles

thick filament

thickening of the left ventricle but can also be the whole heart,could be a defect
in myosin, tropnin, can cause arthemias
ventricles are enlarged (bigger chambers), defect specific in ALPHA-ACTIN

No sarcomere

signal casacade, second messengers

etc.
alpha actin acts as a Z-disc, but smooth muscle does not
have a z-disc

in smooth muscle

inhinders myosin and actin from binding

myosine light chain kinase - when light chains are phosphorylated, it allows the heavy
chains to unfold and allows us to get an active form to allow for contraction
VERY HIGH YEILD!!!

myosin
phosphorylates light chains of myosin-unfodls and
expose ATPas head and contracts

released from SR
allowing myosin and actin to bind

myosin light chain kinase

protein kinase-C, which phosporylates MLCK

Diaceyl-glyceral

CAMP and DAG lead to smooth muscle relaxtion by phosphrylating the inactive forms

in telophase and cytokineses

bundle actin filaments

connecting actin to the

walls of the microvilli

in the terminal web, and spectrin and myosin 2

crosslink each other

moving towards a chemical gradient ex:leukocyte

These are drugs:
blocks cell movment by bdining to positive end therefore no polymerization
blocks cell movemebt by binding to negative end so cannot depolymerize

remember its a tetramer!

important!

reduced spectrin binding to proteina and reduces cross-linking

(weakens cross-linking)

spectrin is alot stronger in sickle-cell and it is more rigid

and it is more stable due to diminished ubqitination
(decrease ubiquitination of spectrin)
your RBC become sphere shaped, defect in spectrin itself and it cannot bind to 4.1
and adducin and you get fragile RBC
RBC are elipotcial shape - having trouble making spectrin tetramers

results in muscle degeneration - issue with dystrophin

member of the spectrin family, it anchors F-actin to the skeletal muscle

mainly a structural role

cross-linking actin
of intermediate filaments
Drugs:

defect in Lamin A, causing premature aging

mitosis - movement of orgnalles

axenene: stack of microtubules

microtubule is 13 protofilaments of heterodimer filaments,

its basically a hallow tube

micortubules are unstable, in order for them to polymerize there are certain criteria we have to meet:
- CAP > deploymerize negative end and polymerization at positive end
blocks micortubule diassembly: we give it patients
for stoping cell division by blocking microtubule dissaembly
because we cant go thru mitosis

not caped, and microtubule depolymerizes

aggregation of micortubules growing out of a complex called y-tubulin ring complex >especially important during mitosis
- microtubules grow towards these arranged microtbules and connect at the connetacore and this is how they depolyreize the cell
this is during ANAPHASE > (because its facilitiated by the -tubulin ring complex)

with GTP, you cap the NEGATIVE END WITH Y-TUBULIN RING COMPLEX
remove a COOH group and stabalizes the microtubules

binding with MAPS

like calsquesterin

ATP dependent

help move things along microtubules, both use ATP Kineside moves int he plus directiona nd Dynein moves
in the negative direction (anterograde and retrograde)

its a kinesin associated protein, helps kinesin bind to micorutbule.. and Dynactin help dynine bind to the protein
has abnormal APP

cross section of cilia/flagella

- cilia are located in the airways,

aids in motility- connects it to the wall,

why the movement happens
connects doublets to wall
connects doublets together

we dont see polymerization or

deplymerization because its pretty
stable
NEXIN
Three types of microtubules
1. kinetchore MT
2. innerpolar MT (overlap)
3. astro MT (little ones that
grow in all the directions)