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A conserved sequence in calmodulin regulated spectrin-associated protein 1 links its interaction with spectrin and calmodulin to neurite outgrowth.

Authors: King, MD  Phillips, GW  Bignone, PA  Hayes, NV  Pinder, JC  Baines, AJ 
Citation: King MD, etal., J Neurochem. 2014 Feb;128(3):391-402. doi: 10.1111/jnc.12462. Epub 2013 Oct 24.
Pubmed: (View Article at PubMed) PMID:24117850
DOI: Full-text: DOI:10.1111/jnc.12462

Calmodulin regulated spectrin-associated protein 1 (CAMSAP1) is a vertebrate microtubule-binding protein, and a representative of a family of cytoskeletal proteins that arose with animals. We reported previously that the central region of the protein, which contains no recognized functional domain, inhibited neurite outgrowth when over-expressed in PC12 cells [Baines et al., Mol. Biol. Evol. 26 (2009), p. 2005]. The CKK domain (DUF1781) binds microtubules and defines the CAMSAP/ssp4 family of animal proteins (Baines et al. 2009). In the central region, three short well-conserved regions are characteristic of CAMSAP-family members. One of these, CAMSAP-conserved region 1 (CC1), bound to both betaIISigma1-spectrin and Ca(2+)/calmodulin in vitro. The binding of Ca(2+)/calmodulin inhibited spectrin binding. Transient expression of CC1 in PC12 cells inhibited neurite outgrowth. siRNA knockdown of CAMSAP1 inhibited neurite outgrowth in PC12 cells or primary cerebellar granule cells: this could be rescued in PC12 cells by wild-type CAMSAP1-enhanced green fluorescent protein, but not by a CC1 mutant. We conclude that CC1 represents a functional region of CAMSAP1, which links spectrin-binding to neurite outgrowth.

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CRRD Object Information
CRRD ID: 8554252
Created: 2014-05-08
Species: All species
Last Modified: 2014-05-08
Status: ACTIVE



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