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|Title:||Identification of a Subunit of a Novel Kleisin-β/SMC Complex as a Potential Substrate of Protein Phosphatase 2A||Authors:||Yeong, F.M.
|Issue Date:||2003||Citation:||Yeong, F.M., Hombauer, H., Mudrak, I., Loregger, T., Ogris, E., Wendt, K.S., Hirota, T., Mechtler, K., Tanaka, K., Peters, J.-M., Marchler-Bauer, A. (2003). Identification of a Subunit of a Novel Kleisin-β/SMC Complex as a Potential Substrate of Protein Phosphatase 2A. Current Biology 13 (23) : 2058-2064. ScholarBank@NUS Repository. https://doi.org/10.1016/j.cub.2003.10.032||Abstract:||Protein phosphatase 2A (PP2A) holoenzymes consist of a catalytic C subunit, a scaffolding A subunit, and one of several regulatory B subunits that recruit the AC dimer to substrates [1, 2]. PP2A is required for chromosome segregation [3-6], but PP2A's substrates in this process remain unknown. To identify PP2A substrates, we carried out a two-hybrid screen with the regulatory B/PR55 subunit. We isolated a human homolog of C. elegans HCP6, a protein distantly related to the condensin subunit hCAP-D2, and we named this homolog hHCP-6. Both C. elegans HCP-6 and condensin are required for chromosome organization and segregation [7-11]. HCP-6 binding partners are unknown, whereas condensin is composed of the structural maintenance of chromosomes proteins SMC2 and SMC4 and of three non-SMC subunits . Here we show that hHCP-6 becomes phosphorylated during mitosis and that its dephosphorylation by PP2A in vitro depends on B/PR55, suggesting that hHCP-6 is a B/PR55-specific substrate of PP2A. Unlike condensin, hHCP-6 is localized in the nucleus in interphase, but similar to condensin, hHCP-6 associates with chromosomes during mitosis. hHCP-6 is part of a complex that contains SMC2, SMC4, kleisin-β, and the previously uncharacterized HEAT repeat protein FLJ20311. hHCP-6 is therefore part of a condensin-related complex that associates with chromosomes in mitosis and may be regulated by PP2A.||Source Title:||Current Biology||URI:||http://scholarbank.nus.edu.sg/handle/10635/38289||ISSN:||09609822||DOI:||10.1016/j.cub.2003.10.032|
|Appears in Collections:||Staff Publications|
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