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PP2A-B' holoenzyme substrate recognition, regulation and role in cytokinesis
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- Wu, Cheng-Guo (författare)
- Univ Wisconsin Madison, McArdle Lab Canc Res, Dept Oncol, Sch Med & Publ Hlth, Madison, WI 53706 USA.; Univ Wisconsin Madison, Biophys Program, Madison, WI 53706 USA.; DuPont Ind Biosci, Genencor Div, 925 Page Mill Rd, Palo Alto, CA 94304 USA
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- Chen, Hui (författare)
- Univ Wisconsin Madison, McArdle Lab Canc Res, Dept Oncol, Sch Med & Publ Hlth, Madison, WI 53706 USA.; DuPont Ind Biosci, Genencor Div, 925 Page Mill Rd, Palo Alto, CA 94304 USA
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- Guo, Feng (författare)
- Univ Wisconsin Madison, McArdle Lab Canc Res, Dept Oncol, Sch Med & Publ Hlth, Madison, WI 53706 USA.; DuPont Ind Biosci, Genencor Div, 925 Page Mill Rd, Palo Alto, CA 94304 USA.; Univ Pittsburgh, Dept Microbiol & Mol Genet, Pittsburgh, PA USA
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- Univ Wisconsin Madison, McArdle Lab Canc Res, Dept Oncol, Sch Med & Publ Hlth, Madison, WI 53706 USA; Univ Wisconsin Madison, Biophys Program, Madison, WI 53706 USA.; DuPont Ind Biosci, Genencor Div, 925 Page Mill Rd, Palo Alto, CA 94304 USA Univ Wisconsin Madison, McArdle Lab Canc Res, Dept Oncol, Sch Med & Publ Hlth, Madison, WI 53706 USA.; DuPont Ind Biosci, Genencor Div, 925 Page Mill Rd, Palo Alto, CA 94304 USA (creator_code:org_t)
- 2017-08-08
- 2017
- Engelska.
- Ingår i: Cell Discovery. - : Springer Science and Business Media LLC. - 2056-5968. ; 3
- Tidskriftsartikel (refereegranskat)
Abstract
Ämnesord
Stäng
- Protein phosphatase 2A (PP2A) is a major Ser/Thr phosphatase; it forms diverse heterotrimeric holoenzymes that counteract kinase actions. Using a peptidome that tiles the disordered regions of the human proteome, we identified proteins containing [LMFI]xx[ILV]xEx motifs that serve as interaction sites for B'-family PP2A regulatory subunits and holoenzymes. The B'-binding motifs have important roles in substrate recognition and in competitive inhibition of substrate binding. With more than 100 novel ligands identified, we confirmed that the recently identified LxxIxEx B'α-binding motifs serve as common binding sites for B' subunits with minor variations, and that S/T phosphorylation or D/E residues at positions 2, 7, 8 and 9 of the motifs reinforce interactions. Hundreds of proteins in the human proteome harbor intrinsic or phosphorylation-responsive B'-interaction motifs, and localize at distinct cellular organelles, such as midbody, predicting kinase-facilitated recruitment of PP2A-B' holoenzymes for tight spatiotemporal control of phosphorylation at mitosis and cytokinesis. Moroever, Polo-like kinase 1-mediated phosphorylation of Cyk4/RACGAP1, a centralspindlin component at the midbody, facilitates binding of both RhoA guanine nucleotide exchange factor (epithelial cell transforming sequence 2 (Ect2)) and PP2A-B' that in turn dephosphorylates Cyk4 and disrupts Ect2 binding. This feedback signaling loop precisely controls RhoA activation and specifies a restricted region for cleavage furrow ingression. Our results provide a framework for further investigation of diverse signaling circuits formed by PP2A-B' holoenzymes in various cellular processes.
Ämnesord
- NATURVETENSKAP -- Biologi -- Bioinformatik och systembiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Bioinformatics and Systems Biology (hsv//eng)
Nyckelord
- CIP2A
- PP2A-B′ holoenzyme
- SLiMs
- centrosome
- cytokinesis
- midbody
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- Wu, Cheng-Guo
- Chen, Hui
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- Yadav, Vikash K
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- Choudhary, Alka
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