Biology:Bbc1
Bbc1 (Mti1p) is a protein expressed in yeasts that is thought to associate with actin networks. Bbc1 stands for Bni1 synthetic lethal and Bee1 (las17) complex member.[1] The alternate name, Mti1p, stands for Myosin tail region-interacting protein.[2] Bbc1 is involved in cytoskeletal regulation during endocytosis. Budding yeast Bbc1 inhibits the activator of the Arp2/3 complex Las17 (WASp homolog).[3] The protein also interacts with the tail of Myosin 1 proteins.[2]
In fission yeast, Bbc1 is considered a WIP family cytoskeletal protein. Bbc1 localizes to actin cortical patches, cell division sites, the cell tip, and the cytosol. Cells with bbc1 gene deletion are viable.[4] Bbc1 is affinity captured by the Nebulin-family actin filament anchoring protein Cyk3[5] and the SMARCAD1 family ATP-dependent DNA helicase Fft3.[4][6] Bbc1 competes with WIP homolog Vrp1 to bind the Myosin 1 tail to regulate actin assembly at endocytic sites.[7]
References
- ↑ "BBC1 | SGD". https://www.yeastgenome.org/locus/S000003557#reference.
- ↑ 2.0 2.1 Mochida, Junko Yamamoto, Takaharu Fujimura-Kamada, Konomi Tanaka, Kazuma (2002). "The novel adaptor protein, Mti1p, and Vrp1p, a homolog of Wiskott-Aldrich syndrome protein-interacting protein (WIP), may antagonistically regulate type I myosins in Saccharomyces cerevisiae.". Genetics 160 (3): 923–34. OCLC 678661938. PMID 11901111.
- ↑ Rodal, Avital A.; Manning, Amity L.; Goode, Bruce L.; Drubin, David G. (June 2003). "Negative Regulation of Yeast WASp by Two SH3 Domain-Containing Proteins". Current Biology 13 (12): 1000–1008. doi:10.1016/s0960-9822(03)00383-x. ISSN 0960-9822. PMID 12814545.
- ↑ 4.0 4.1 "Pombase". https://www.pombase.org/gene/SPAC23A1.17.
- ↑ Roberts-Galbraith, Rachel H.; Ohi, Melanie D.; Ballif, Bryan A.; Chen, Jun-Song; McLeod, Ian; McDonald, W. Hayes; Gygi, Steven P.; Yates, John R. et al. (2010-07-09). "Dephosphorylation of F-BAR protein Cdc15 modulates its conformation and stimulates its scaffolding activity at the cell division site". Molecular Cell 39 (1): 86–99. doi:10.1016/j.molcel.2010.06.012. ISSN 1097-4164. PMID 20603077. PMC 2916701. https://www.ncbi.nlm.nih.gov/pubmed?holding=pombase&term=20603077.
- ↑ Lee, Junwoo; Choi, Eun Shik; Seo, Hogyu David; Kang, Keunsoo; Gilmore, Joshua M.; Florens, Laurence; Washburn, Michael P.; Choe, Joonho et al. (February 20, 2017). "Chromatin remodeller Fun30Fft3 induces nucleosome disassembly to facilitate RNA polymerase II elongation". Nature Communications 8: 14527. doi:10.1038/ncomms14527. ISSN 2041-1723. PMID 28218250. PMC 5321744. Bibcode: 2017NatCo...814527L. https://www.ncbi.nlm.nih.gov/pubmed?holding=pombase&term=28218250.
- ↑ MacQuarrie, Cameron Dale; Mangione, MariaSanta C.; Carroll, Robert; James, Michael; Gould, Kathleen L.; Sirotkin, Vladimir (2019-08-07). "The S. pombe adaptor protein Bbc1 regulates localization of Wsp1 and Vrp1 during endocytic actin patch assembly". Journal of Cell Science 132 (17): jcs233502. doi:10.1242/jcs.233502. ISSN 0021-9533. PMID 31391237.
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