Protein serine/threonine phosphatases; an expanding family
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TLDR
Five protein serine/threonine phosphatases (PP) have been identified by cloning cDNA from mammalian and Drosophila libraries and the complete amino acid sequences of PPX, PPY and PPZ and an almost complete sequence of PPV are presented.About:
This article is published in FEBS Letters.The article was published on 1990-08-01 and is currently open access. It has received 211 citations till now. The article focuses on the topics: Protein tyrosine phosphatase & Protein phosphorylation.read more
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The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit.
Tim Durfee,Kathleen Becherer,Phang Lang Chen,Shiou-Hwei Yeh,Yanzhu Yang,April E. Kilburn,Wen-Hwa Lee,Stephen J. Elledge +7 more
TL;DR: An improved version of the yeast two-hybrid system is developed and used to isolate human cDNAs encoding proteins able to bind p110RB to demonstrate that PP-1 alpha isoforms preferentially bind the hypophosphorylated form of p110 RB.
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Protein serine/threonine phosphatases--new avenues for cell regulation.
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The SIT4 protein phosphatase functions in late G1 for progression into S phase.
A. Sutton,D Immanuel,K T Arndt +2 more
TL;DR: Order-of-function analysis shows that SIT4 is required in late G1 for progression into S phase, and identifies a polymorphic gene, SSD1, that in some versions can suppress the lethality due to a deletion of S IT4 and can also partially suppress the phenotypic defectsDue to a null mutation in BCY1.
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Differential inactivation of postsynaptic density-associated and soluble Ca2+/calmodulin-dependent protein kinase II by protein phosphatases 1 and 2A.
TL;DR: In this article, protein phosphatase classes responsible for dephosphorylation of Ca2+/calmodulin-dependent protein kinase II (CaMKII) at Thr286 were identified using rat forebrain subcellular fractions.
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Structure of Protein Phosphatase 2A Core Enzyme Bound to Tumor-Inducing Toxins
Yongna Xing,Yanhui Xu,Yu Chen,Philip D. Jeffrey,Yang Chao,Zheng Lin,Zhu Li,Stefan Strack,Jeffry B. Stock,Yigong Shi +9 more
TL;DR: The crystal structures of the PP2A core enzyme bound to two of its inhibitors, the tumor-inducing agents okadaic acid and microcystin-LR, are reported at 2.6 and 2.8 A resolution and serve as a framework for deciphering the diverse roles ofPP2A in cellular physiology.
References
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The structure and regulation of protein phosphatases
TL;DR: Four major serine/threonine-specific protein phosphatase catalytic subunits are present in the cytoplasm of animal cells and have broad and overlapping specificities in vitro, and account for virtually all measurable activity in tissue extracts toward a variety of phosphoproteins that regulate metabolism, muscle contractility, and other processes.
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Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics
Corinna Bialojan,Akira Takai +1 more
TL;DR: Kinetic studies showed that okadaic acid acts as a non-competitive or mixed inhibitor on the okadaIC acid-sensitive enzymes.
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Cyanobacterial microcystin-LR is a potent and specific inhibitor of protein phosphatases 1 and 2A from both mammals and higher plants.
TL;DR: The cyclic heptapeptide, microcystin‐LR, inhibits protein phosphatases 1 (PP1) and 2A (PP2A) with K i, values below 0.1 nM, and this results are strikingly similar to those obtained with the tumour promoter okadaic acid.
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Protein Serine/Threonine Kinases
TL;DR: D OUBLE-S TRAND ED RNA-D EPENDEN T PROTEIN KINASE and J3-ADR ENERGIC REC EPTOR KINAS.
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Okadaic acid: a new probe for the study of cellular regulation.
TL;DR: The tumour promoter okadaic acid is a potent and specific inhibitor of protein phosphatases 1 and 2A and is extremely useful for identifying biological processes that are controlled through the reversible phosphorylation of proteins.