Cargando…
CARMIL leading edge localization depends on a non-canonical PH domain and dimerization
CARMIL is a ~1370 amino acid cytoskeletal scaffold that plays crucial roles in cell motility and tissue development through interactions with cytoskeletal effectors and regulation of capping protein at the leading edge. However, the mechanism of CARMIL leading edge localization is unknown. Here we s...
Autores principales: | Zwolak, Adam, Yang, Changsong, Feeser, Elizabeth A., Ostap, E. Michael, Svitkina, Tatyana, Dominguez, Roberto |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3796438/ https://www.ncbi.nlm.nih.gov/pubmed/24071777 http://dx.doi.org/10.1038/ncomms3523 |
Ejemplares similares
-
PICK1 is implicated in organelle motility in an Arp2/3 complex–independent manner
por: Madasu, Yadaiah, et al.
Publicado: (2015) -
Mechanisms of plasma membrane targeting of formin mDia2 through its amino terminal domains
por: Gorelik, Roman, et al.
Publicado: (2011) -
WAVE1 and WAVE2 have distinct and overlapping roles in controlling actin assembly at the leading edge
por: Tang, Qing, et al.
Publicado: (2020) -
Dual regulation of the actin cytoskeleton by CARMIL-GAP
por: Jung, Goeh, et al.
Publicado: (2022) -
A Novel Pathogenic Variant in CARMIL2 (RLTPR) Causing CARMIL2 Deficiency and EBV-Associated Smooth Muscle Tumors
por: Yonkof, Jennifer R., et al.
Publicado: (2020)