A PP2A-B55 recognition signal controls substrate dephosphorylation kinetics during mitotic exit.
about
Protein phosphatase 2A regulatory subunit B55α functions in mouse oocyte maturation and early embryonic development.PP2ACdc55 Phosphatase Imposes Ordered Cell-Cycle Phosphorylation by Opposing Threonine Phosphorylation.Express yourself: how PP2A-B55(Pab1) helps TORC1 talk to TORC2.Mitotic exit: Determining the PP2A dephosphorylation programCoupling TOR to the Cell Cycle by the Greatwall-Endosulfine-PP2A-B55 Pathway.AMPK regulates anaphase central spindle length by phosphorylation of KIF4A.Distinct kinetics of serine and threonine dephosphorylation are essential for mitosis.Interlinked bistable mechanisms generate robust mitotic transitions.Protein interactomes of protein phosphatase 2A B55 regulatory subunits reveal B55-mediated regulation of replication protein A under replication stress.Protein phosphatases at the nuclear envelope.Phosphoproteome dynamics during mitotic exit in budding yeast.CDK1 and PLK1 coordinate the disassembly and reassembly of the nuclear envelope in vertebrate mitosis.SILAC-based phosphoproteomics reveals new PP2A-Cdc55-regulated processes in budding yeast.Coordination of Protein Kinase and Phosphoprotein Phosphatase Activities in Mitosis.MASTL overexpression promotes chromosome instability and metastasis in breast cancer.Dephosphorylation of the HIV-1 restriction factor SAMHD1 is mediated by PP2A-B55α holoenzymes during mitotic exit.Kinase and Phosphatase Cross-Talk at the Kinetochore.The dNTP triphosphohydrolase activity of SAMHD1 persists during S-phase when the enzyme is phosphorylated at T592
P2860
Q33688896-8E76BE44-D029-4B60-A221-C6A6B883DAB0Q37629763-72226467-5B1A-4479-9AB4-295175CF39F2Q38667730-A6EBCE18-E747-4EBC-809D-88CEB9E55886Q40973101-D1A8925A-0DA6-4E49-95E8-8F32FE524E69Q41663539-D703B01C-6074-4AE3-9628-445BBEC21450Q41921520-2719782C-06E8-4C59-B896-09F6824F0ED4Q47588118-DF9C1B7B-2262-4CBA-BA9C-49FB5D4DE4FAQ47688687-0ADB1BF5-93DE-4E94-9F9A-A64FFF688A38Q49380019-C7084586-7AF5-4040-BC87-FD648E59C759Q50047443-12F95C6D-7AB2-4781-869B-59414AE6FCAFQ52323108-AAD1A2C7-4F9F-4A92-B787-B78CCACFF592Q52371900-9FF7239A-84A8-4B56-825D-26D7D45C1446Q52567318-7D743E4F-9C37-4A6D-B469-5E18D0C4FDC7Q52721214-A2EDB85A-C9EE-441E-8415-AC59989FEEB3Q54979446-FD3206AB-B3DD-4443-B01B-50E6B0AB4BE1Q55178348-B7ABCDEE-EBF4-44A7-8FB8-3A3A121625F2Q55512020-02C778BD-995A-4B68-8268-1469C4F40D4FQ57383768-7802197B-A1D8-4422-B2F2-40FE8911A370
P2860
A PP2A-B55 recognition signal controls substrate dephosphorylation kinetics during mitotic exit.
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
2016年论文
@zh
2016年论文
@zh-cn
name
A PP2A-B55 recognition signal ...... kinetics during mitotic exit.
@en
type
label
A PP2A-B55 recognition signal ...... kinetics during mitotic exit.
@en
prefLabel
A PP2A-B55 recognition signal ...... kinetics during mitotic exit.
@en
P2860
P50
P356
P1476
A PP2A-B55 recognition signal ...... n kinetics during mitotic exit
@en
P2093
Michael J Cundell
P2860
P304
P356
10.1083/JCB.201606033
P407
P50
P577
2016-08-22T00:00:00Z