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

King, Mikayala D.A., Phillips, Gareth W., Bignone, Paola A., Hayes, Nandini V. L., Pinder, Jennifer C., Baines, Anthony J. (2013) A conserved sequence in calmodulin regulated spectrin-associated protein 1 links its interaction with spectrin and calmodulin to neurite outgrowth. Journal of Neurochemistry, 128 (3). pp. 391-402. ISSN 0022-3042. E-ISSN 1471-4159. (doi:10.1111/jnc.12462) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Official URL
http://dx.doi.org/10.1111/jnc.12462

Abstract

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 ?II?1-spectrin and Ca2+/calmodulin in vitro. The binding of Ca2+/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.

Item Type: Article
DOI/Identification number: 10.1111/jnc.12462
Uncontrolled keywords: nerve cells; molecular evolution; protein domain; cytoskeleton; cytoskeletal regulation; protein function.
Subjects: Q Science > QP Physiology (Living systems) > QP506 Molecular biology
Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Anthony Baines
Date Deposited: 13 Nov 2013 15:58 UTC
Last Modified: 29 May 2019 11:20 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/36298 (The current URI for this page, for reference purposes)
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