Cytoskeleton (IF and MT) Flashcards
Generic kinesin structure
motor (head) domain = contains ATP binding site + MT binding site, determines movement
neck = flexible region connecting motor domain to central stalk, determines direction
Kinesin 1
~ globular bulbous region (motor domain) at one end of the molecule
~ region is enlarged when specific antibody present
Function: organelle transport
Kinesin 5
~ two bulbous regions - one at each end of the molecule (bipolar kinesin)
~ tetramer (two dimers joined together by tails overlapping)
Function: involved with sliding MT overreach in mitotic spindle
Dyneins
~ MT motor protein
~ move cargo towards -ve end of MT (retrograde)
~ linked to cargo by dynactin
Dynein structure
~ dynactin binding domain
~ ATPase domain (x2)- circular with 6 sections
~ microtubule binding domain (one per ATPase) a.k.a. feet
Dynactin
contains CapZ and dynamitin
Multi-directional cargo
~ some cargos are able to move in both directions –> have kinesin and dynein but only one is active at a time
e.g. pigment granules + mitochondria
What speed does kinesin travel at?
600nm per second = slow
Axoneme
core of cilia and flagella
~ made of 9 outer MT doublets and a central pair (9 +2 arrangement)
~ each outer doublet = 1 13 protofilament and 1 10 protofilament
~ centraal doublet = 13 protofilaments
~ cell movement depends on axoneme bending
Kinetochore MT
connect chromo. to spindle poles (kinetochore attachment site)
What microtubules are in spindle?
Kinetochore MT = connect chromo. to spindle poles (kinetochore attachment site)
Polar MT = overlap and hold the poles together and regulate their distance
Astral MT = from spinal pole towards cell cortex, help to position the spindle
Polar MT
overlap and hold the poles together and regulate their distance
Intermediate filaments
protein subunits that make a strong rope-like polymers that provide mechanical support or cell adhesion
e.g. keratin + lamin
IF structure
~ globular N-terminal and C-terminal domains connected by a central, helical core
~ the core = conserved among all IF, mediates dimer and tetramer formation
Multi-IF structure
~ form protofilaments (out of tetramers)
~ 2 protofilaments form a protofibril
~ 4 protofirbil wind around each other = rope structure