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How do bacteria, such as listeria, hijack host actin cytoskeleton
ActA in bacteria can activate Arp 2/3
result:polymerization at surface of bacteria so it can now be displaced / moved
can also recruit coffin to sever old actin at the minus end so that we can remain at Cc and keep adding to the plus end
what kind of actin can push the membrane forward
branched actin
activation of ARP 2/3 change dynamics of plasma membrane
name some key differences between the protrusive actin structures filopodia and lamellipodia
filopodia:
sent out first to make sure things are going in the right direction
unbranched → formin
finger like protrusions
CDC42
Lamellipodia
sheets that protrude
branched → ARP 2/3
Rac
what is a stress fiber
a contractile bundle that is unbranched (therefore formin nucleated) and is associated with non muscle myosin
briefly describe cell crawling
protrusion, attachment, contraction
actin polymerization at plus end protrudes lamellipdium
integrin help attach to substratum/ECM
stress fibers in back allow for actin myosin contraction
what is the function of integrins
they link the cytoskeleton and ECM/substratum
active when stretched out
link through focal adhesions
Summarize how different members of the Rho family of GTPases alter the organization of actin filaments.
Rho: promotes stress fibers (contractile actin)
effector: whatever controls actin myosin contractility
rho must be in back for directionality (visualize how the cell crawls)
Rac: promotes lemellipodial extension
effector: ARP 2/3
must be in front for protrusion
CDC42: promotes filipodia
effector: formin
must go first in front to make sure everything is in correct direction
initiates actin polymerization
what would occur if Rho was mutated
this would affect cell crawling
double negative: locked in the inactive GDP bound state
how do Rho family GTPases promote actin filament nucleation
they stimulate profiling-bound actin recruitment to NPF/WAVE and forming
WASP/WAVE/NPF os activated downstream of ______ leading to Rac activation and ____ generation at cell edge
CDC42
PI(4,5)P2