Document Detail

A kinesin-1 binding motif in vaccinia virus that is widespread throughout the human genome.
MedLine Citation:
PMID:  21915095     Owner:  NLM     Status:  MEDLINE    
Transport of cargoes by kinesin-1 is essential for many cellular processes. Nevertheless, the number of proteins known to recruit kinesin-1 via its cargo binding light chain (KLC) is still quite small. We also know relatively little about the molecular features that define kinesin-1 binding. We now show that a bipartite tryptophan-based kinesin-1 binding motif, originally identified in Calsyntenin is present in A36, a vaccinia integral membrane protein. This bipartite motif in A36 is required for kinesin-1-dependent transport of the virus to the cell periphery. Bioinformatic analysis reveals that related bipartite tryptophan-based motifs are present in over 450 human proteins. Using vaccinia as a surrogate cargo, we show that regions of proteins containing this motif can function to recruit KLC and promote virus transport in the absence of A36. These proteins interact with the kinesin light chain outside the context of infection and have distinct preferences for KLC1 and KLC2. Our observations demonstrate that KLC binding can be conferred by a common set of features that are found in a wide range of proteins associated with diverse cellular functions and human diseases.
Mark P Dodding; Richard Mitter; Ashley C Humphries; Michael Way
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The EMBO journal     Volume:  30     ISSN:  1460-2075     ISO Abbreviation:  EMBO J.     Publication Date:  2011 Nov 
Date Detail:
Created Date:  2011-12-22     Completed Date:  2012-01-20     Revised Date:  2013-06-27    
Medline Journal Info:
Nlm Unique ID:  8208664     Medline TA:  EMBO J     Country:  England    
Other Details:
Languages:  eng     Pagination:  4523-38     Citation Subset:  IM    
Cell Motility Laboratory, London Research Institute, Cancer Research UK, London, UK.
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MeSH Terms
Amino Acid Motifs
Biological Transport
Calcium-Binding Proteins / chemistry,  metabolism
Cell Line
Genome, Human
HeLa Cells
Kinesin / chemistry,  genetics,  metabolism*
Microtubule-Associated Proteins / chemistry*,  metabolism*
Protein Binding
Protein Structure, Tertiary
Sequence Alignment
Tryptophan / chemistry
Vaccinia virus / chemistry*,  genetics,  physiology*
Viral Matrix Proteins / chemistry*,  genetics,  metabolism*
Virus Release
Reg. No./Substance:
0/CLSTN1 protein, human; 0/Calcium-Binding Proteins; 0/KIF5B protein, human; 0/Microtubule-Associated Proteins; 0/Viral Matrix Proteins; 0/kinesin light-chain proteins; 73-22-3/Tryptophan; EC 3.6.1.-/Kinesin

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