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SCF-Fbxo42 promotes synaptonemal complex assembly by downregulating PP2A-B56
Author(s) -
Pedro Barbosa,
Liudmila Zhaunova,
Simona Debilio,
Verdiana Steccanella,
Van Kelly,
Tony Ly,
Hiroyuki Ohkura
Publication year - 2020
Publication title -
the journal of cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.414
H-Index - 380
eISSN - 1540-8140
pISSN - 0021-9525
DOI - 10.1083/jcb.202009167
Subject(s) - synaptonemal complex , biology , microbiology and biotechnology , meiosis , ubiquitin ligase , protein subunit , homologous chromosome , protein phosphatase 2 , chromosome segregation , meiosis ii , genetics , phosphorylation , ubiquitin , chromosome , phosphatase , gene
Meiosis creates genetic diversity by recombination and segregation of chromosomes. The synaptonemal complex assembles during meiotic prophase I and assists faithful exchanges between homologous chromosomes, but how its assembly/disassembly is regulated remains to be understood. Here, we report how two major posttranslational modifications, phosphorylation and ubiquitination, cooperate to promote synaptonemal complex assembly. We found that the ubiquitin ligase complex SCF is important for assembly and maintenance of the synaptonemal complex in Drosophila female meiosis. This function of SCF is mediated by two substrate-recognizing F-box proteins, Slmb/βTrcp and Fbxo42. SCF-Fbxo42 down-regulates the phosphatase subunit PP2A-B56, which is important for synaptonemal complex assembly and maintenance.

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