Slow axonal transport of the cytosolic chaperonin CCT with Hsc73 and actin in motor neurons

Carden, Martin J. and Roobol, Anne and El Alami, Wathik and Wilson, Suzanne J. and Bourke, Gregory J. (2002) Slow axonal transport of the cytosolic chaperonin CCT with Hsc73 and actin in motor neurons. Journal of Neuroscience Research, 68 (1). pp. 29-35. ISSN 0360-4012. (The full text of this publication is not available from this repository)

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Official URL
http:dx.doi.org/10.1002/jnr.10186

Abstract

Molecular chaperones are well known for their role in facilitating the folding of nascent and newly synthesized proteins, but have other roles, including the assembly, translocation and renaturation of intracellular proteins. Axons are convenient tissues for the study of some of these other roles because they lack the capacity for significant protein synthesis. We examine the axonal transport of the cytosolic chaperonin containing T- complex polypeptide 1 (CCT) by labeling lumbar motor neurons with [35S]methionine and examining sciatic nerve proteins by 2-D gel electrophoresis and immunoblotting. All CCT subunits identifiable with specific antibodies, namely CCTα, CCTβ, CCTγ and CCTϵ/CCTθ (the latter two subunits colocalized in analyses of rat nerve samples), appeared to be labeled in “slow component b” of axonal transport along with the molecular chaperone Hsc73 and actin, a major folding substrate for CCT. Our results are consistent with molecular chaperones having a post-translational role in maintaining the native form of actin during its slow transport to the axon terminal and ensuring its correct assembly into microfilaments. © 2002 Wiley-Liss, Inc.

Item Type: Article
Uncontrolled keywords: actin; chaperonin containing T-complex polypeptide 1; heat shock protein 70; axons; slow axonal transport
Subjects: Q Science > Q Science (General)
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: P. Ogbuji
Date Deposited: 09 Apr 2009 11:47
Last Modified: 28 Apr 2014 15:19
Resource URI: http://kar.kent.ac.uk/id/eprint/16215 (The current URI for this page, for reference purposes)
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