3FGA

Structural Basis of PP2A and Sgo interaction

Summary for 3FGA

• Entry DOI: 10.2210/pdb3fga/pdb
• Related PRD ID: PRD_000212
• Descriptor: Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform, Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform, Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform, ... (7 entities in total)
• Functional Keywords: pp2a, shugoshin, nucleus, phosphoprotein, hydrolase, iron, manganese, metal-binding, methylation, protein phosphatase, cell cycle, cell division, centromere, chromosome partition, mitosis, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Mus musculus (mouse); More
• Cellular location: Cytoplasm : Q76MZ3 P67775; Nucleus: Q13362 Q5FBB7
• Total number of polymer chains: 5
• Total formula weight: 155274.26

Authors

Xu, Z.,Xu, W. (deposition date: 2008-12-05, release date: 2009-09-22, Last modification date: 2023-11-15)

Primary citation

Xu, Z.,Cetin, B.,Anger, M.,Cho, U.S.,Helmhart, W.,Nasmyth, K.,Xu, W.
Structure and function of the PP2A-shugoshin interaction
Mol.Cell, 35:426-441, 2009

PubMed Abstract: Accurate chromosome segregation during mitosis and meiosis depends on shugoshin proteins that prevent precocious dissociation of cohesin from centromeres. Shugoshins associate with PP2A, which is thought 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 PP2A holoenzyme reveals that Sgo1 forms a homodimeric parallel coiled coil that docks simultaneously onto PP2A's C and B' subunits. Sgo1 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 in 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 sufficient to protect cohesin from separase in mammalian oocytes.

PubMed: 19716788
DOI: 10.1016/j.molcel.2009.06.031

Experimental method

X-RAY DIFFRACTION (2.7 Å)