Unknown

Dataset Information

0

CR16 forms a complex with N-WASP in brain and is a novel member of a conserved proline-rich actin-binding protein family.


ABSTRACT: The Neuronal Wiskott-Aldrich syndrome protein (N-WASP) has emerged as a central regulator of the actin cytoskeleton with abilities to integrate multiple upstream signal inputs and transmit them to the Arp2/3 complex. Here, we demonstrate that native N-WASP is present in a tight complex with a proline-rich protein, CR16, which shares approximately 25% identity with WASP interacting protein. CR16 is encoded by a gene previously cloned as a glucocorticoid-regulated mRNA from a rat hippocampal cDNA library. Although N-WASP is expressed ubiquitously, full-length CR16 protein is found predominately in the brain. CR16 and N-WASP colocalize in primary hippocampal neurons and at the tips of their growth cone filopodia. In vitro, CR16 directly binds both monomeric and filamentous actin but does not affect the kinetics of actin polymerization mediated by N-WASP and the Arp2/3 complex. Sequence homologues of CR16 are found not only in other vertebrates but also in the invertebrate Caenorhabditis elegans and in yeast. Thus, CR16 and WASP interacting protein belong to a family of N-WASP-binding proteins.

SUBMITTER: Ho HY 

PROVIDER: S-EPMC58725 | BioStudies | 2001-01-01

REPOSITORIES: biostudies

Similar Datasets

2001-01-01 | S-EPMC2196001 | BioStudies
2011-01-01 | S-EPMC3158169 | BioStudies
2008-01-01 | S-EPMC2680354 | BioStudies
2008-01-01 | S-EPMC2414292 | BioStudies
2010-01-01 | S-EPMC3017724 | BioStudies
2018-01-01 | S-EPMC6292448 | BioStudies
2005-01-01 | S-EPMC1283820 | BioStudies
1000-01-01 | S-EPMC2580791 | BioStudies
2004-01-01 | S-EPMC1224166 | BioStudies
1000-01-01 | S-EPMC2525560 | BioStudies