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

Cristina Polinsky | Zendy; Chanelle Houston | Zendy; Jaynine Vado | Zendy; Azizahmed Shaikh | Zendy; Rebecca Kohn | Zendy

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

Author(s) -

Cristina Polinsky,

Chanelle Houston,

Jaynine Vado,

Azizahmed Shaikh,

Rebecca Kohn

Publication year - 2006

Publication title -

acta biochimica polonica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.452

H-Index - 78

eISSN - 1734-154X

pISSN - 0001-527X

DOI - 10.18388/abp.2006_3372

Subject(s) - proteasome , caenorhabditis elegans , drosophila melanogaster , microbiology and biotechnology , rna splicing , yeast , protein degradation , f box protein , biology , exonuclease , rna binding protein , function (biology) , biochemistry , ubiquitin , rna , gene , ubiquitin ligase , dna polymerase

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.

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