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Synaptic protein UNC-13 interacts with an F-box protein that may target it for degradation by proteasomes.
- 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.
- Subjects :
- Animals
Caenorhabditis elegans
Caenorhabditis elegans Proteins metabolism
Carrier Proteins
Drosophila melanogaster
Exonucleases metabolism
Neurotransmitter Agents chemistry
Protein Binding
Protein Structure, Tertiary
Transgenes
Two-Hybrid System Techniques
Caenorhabditis elegans Proteins chemistry
F-Box Proteins chemistry
Gene Expression Regulation
Proteasome Endopeptidase Complex metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0001-527X
- Volume :
- 53
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Acta biochimica Polonica
- Publication Type :
- Academic Journal
- Accession number :
- 16496042