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SUMMARY:Regulation of actin-binding proteins mediated by lipid-protein int
 eractions
DTSTART;VALUE=DATE-TIME:20260326T130500Z
DTEND;VALUE=DATE-TIME:20260326T132500Z
DTSTAMP;VALUE=DATE-TIME:20260425T232449Z
UID:indico-contribution-10345@events.saip.org.za
DESCRIPTION:Speakers: Yosuke Senju ()\nThe actin cytoskeleton drives membr
 ane deformation during many cellular processes\, such as migration\, morph
 ogenesis\, and endocytosis. Phosphatidylinositol 4\,5-bisphosphate [PI(4\,
 5)P2]\, one of the phosphoinositides\, regulates the activities of many ac
 tin-binding proteins (ABPs)\, including profilin\, cofilin\, Dia2\, N-WASP
 \, ezrin\, and moesin\; however\, the underlying molecular mechanisms rema
 in elusive. Here\, we applied a combination of biophysical assays and atom
 istic molecular dynamics simulations to uncover the molecular principles u
 nderlying ABP interactions with phosphoinositide-containing membranes. Our
  results reveal that these proteins show significant differences in membra
 ne interaction dynamics and in the ranges of phosphoinositide densities th
 ey can sense. Profilin and cofilin show transient\, low-affinity interacti
 ons with membranes\, whereas F-actin assembly factors Dia2 and N-WASP stay
  on membranes longer to perform their functions. Ezrin and moesin\, which 
 link the actin cytoskeleton to the plasma membrane\, bind to membranes wit
 h high affinity and slow dissociation kinetics\, regulating PI(4\,5)P2 lat
 eral diffusion. Unlike profilin\, cofilin\, Dia2\, and N-WASP\, they do no
 t require a high ‘stimulus-responsive’ phosphoinositide density for me
 mbrane binding. Together\, these findings demonstrate that the membrane-in
 teraction mechanisms of ABPs have evolved to precisely fulfill their speci
 fic cellular functions in cytoskeletal dynamics.\n\nhttps://events.saip.or
 g.za/event/272/contributions/10345/
LOCATION:
URL:https://events.saip.org.za/event/272/contributions/10345/
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