CRMP-1 enhances EVL-mediated actin elongation to build lamellipodia and the actin cortex
نویسندگان
چکیده
منابع مشابه
CRMP-1 enhances EVL-mediated actin elongation to build lamellipodia and the actin cortex
Cells can control actin polymerization by nucleating new filaments or elongating existing ones. We recently identified CRMP-1 as a factor that stimulates the formation of Listeria monocytogenes actin comet tails, thereby implicating it in actin assembly. We now show that CRMP-1 is a major contributor to actin assembly in epithelial cells, where it works with the Ena/VASP family member EVL to as...
متن کاملMyosin 1E localizes to actin polymerization sites in lamellipodia, affecting actin dynamics and adhesion formation
Because the actin network in active lamellipodia is continuously assembling at the edge, moving inward and disassembling, there is a question as to how actin-binding proteins and other components are transported to the leading edge and how nascent adhesions are stabilized. Active transport could play a significant role in these functions but the components involved are unknown. We show here tha...
متن کاملCRMP-5 interacts with actin to regulate neurite outgrowth
CRMP family proteins (CRMPs) are abundantly expressed in the developing nervous system mediating growth cone guidance, neuronal polarity and axon elongation. CRMP‑5 has been indicated to serve a critical role in neurite outgrowth. However, the detailed mechanisms of how CRMP‑5 regulates neurite outgrowth remain unclear. In the current study, co-immunoprecipitation was used to identify the fact ...
متن کاملActin branching in the initiation and maintenance of lamellipodia.
Using correlated live-cell imaging and electron tomography we found that actin branch junctions in protruding and treadmilling lamellipodia are not concentrated at the front as previously supposed, but link actin filament subsets in which there is a continuum of distances from a junction to the filament plus ends, for up to at least 1 μm. When branch sites were observed closely spaced on the sa...
متن کاملMolecular mechanism of Ena/VASP-mediated actin-filament elongation
Ena/VASP proteins are implicated in a variety of fundamental cellular processes including axon guidance and cell migration. In vitro, they enhance elongation of actin filaments, but at rates differing in nearly an order of magnitude according to species, raising questions about the molecular determinants of rate control. Chimeras from fast and slow elongating VASP proteins were generated and th...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 2017
ISSN: 0021-9525,1540-8140
DOI: 10.1083/jcb.201606084