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Synaptic protein UNC-13 interacts with an F-box protein that may target it for degradation by proteasomes.

Authors :
Polinsky C
Houston C
Vado J
Shaikh A
Kohn RE
Source :
Acta biochimica Polonica [Acta Biochim Pol] 2006; Vol. 53 (1), pp. 145-8. Date of Electronic Publication: 2006 Feb 23.
Publication Year :
2006

Abstract

UNC-13 protein participates in regulating neurotransmitter release. In Drosophila melanogaster, proteasomal degradation controls UNC-13 levels at synapses. Function of the amino-terminal region of a 207 kDa form of Caenorhabditis elegans UNC-13 is unknown. Yeast two-hybrid and secondary yeast assays identified an F-box protein that interacts with this amino-terminal region. As F-box proteins bind proteins targeted for proteasomal degradation, this protein may participate in degrading a subset of UNC-13 proteins, suggesting that different forms of UNC-13 are regulated differently. Yeast assays also identified an exonuclease, a predicted splicing factor, and a protein with coiled-coil domains, indicating that UNC-13 may affect RNA function.

Details

Language :
English
ISSN :
0001-527X
Volume :
53
Issue :
1
Database :
MEDLINE
Journal :
Acta biochimica Polonica
Publication Type :
Academic Journal
Accession number :
16496042