Structure and function of the PP2A-shugoshin interaction

0328951 - ÚŽFG 2010 RIV US eng J - Journal Article
Xu, Z. - Cetin, B. - Anger, Martin - Cho, U. S. - Helmhart, W. - Nasmyth, K. - Xu, W.
Structure and function of the PP2A-shugoshin interaction.
Molecular Cell. Roč. 35, č. 4 (2009), s. 426-441. ISSN 1097-2765. E-ISSN 1097-4164
Institutional research plan: CEZ:AV0Z50450515
Keywords : oocytes * PP2A-Shugoshin * mitosis
Subject RIV: EB - Genetics ; Molecular Biology
Impact factor: 14.608, year: 2009

Accurate chromosome segregation during mitosis and meiosis depends od shugoshin proteins that prevent precocious dissociatin of cohesin from centromeres. Shugoshins associate with PP2A, which is trought to dephosphorylate cohesin and thereby prevent cleavage by separase during meiosis I. A crystal structure of a complex between a fragment of human Sgo1 and an AB.C PP1A holoenzyme reveals that Sgo1 forms a homodimerization is a prerequisite for PP2A binding. While hSgo1 interacts only with the AB.C holoenzymes, its relative, Sgo2 interacts with all PP2A forms and may thus lead to dephosphorylation of distinct substrates. Mutant shugoshin proteins defective id the binding of PP2A cannot protect centromeric cohesin from separase during meiosis I or support the spindle assembly checkpoint in yeast. Finally, we provide evidence that PP2A´s recruitment to chromosomes may be sufficied to protect cohesin from separase in mammalian oocytes.
Permanent Link: http://hdl.handle.net/11104/0175123