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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. 
Hombauer, H.
Mudrak, I.
Loregger, T.
Ogris, E.
Wendt, K.S.
Hirota, T.
Mechtler, K.
Tanaka, K.
Peters, J.-M.
Marchler-Bauer, A.
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.
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 [12]. 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
ISSN: 09609822
DOI: 10.1016/j.cub.2003.10.032
Appears in Collections:Staff Publications

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