Details

Autor(en) / Beteiligte

• Ho, Hsin-Yi Henry
• Rohatgi, Rajat
• Ma, Le
• Kirschner, Marc W.

Titel

CR16 Forms a Complex with N-WASP in Brain and is a Novel Member of a Conserved Proline-Rich Actin-Binding Protein Family

Ist Teil von

• Proceedings of the National Academy of Sciences - PNAS, 2001-09, Vol.98 (20), p.11306-11311

Ort / Verlag

United States: National Academy of Sciences

Erscheinungsjahr

2001

Quelle

Free E-Journal (出版社公開部分のみ）

Beschreibungen/Notizen

• 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 ≈25% identity with WASP interacting protein. CR16 is encoded by a gene previously cloned as a glucocorticoidregulated 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.