Identification and Characterization of the Human HCG V Gene Product as a Novel Inhibitor of Protein Phosphatase-1†

Biochemistry ◽  
1998 ◽  
Vol 37 (47) ◽  
pp. 16728-16734 ◽  
Author(s):  
Jun Zhang ◽  
Lifang Zhang ◽  
Sumin Zhao ◽  
Ernest Y. C. Lee
Keyword(s):  
Gene Product ◽  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
V Gene ◽  
Identification And Characterization

scholarly journals Identification and characterization of phostensin, a protein phosphatase 1 F‐actin cytoskeleton targeting subunit

2009 ◽  
Vol 23 (S1) ◽  
Author(s):  
Tzu‐Fan Wang ◽  
Shu‐Chen Kao ◽  
Shiu‐Lan Wang ◽  
Chun‐Yu Chen ◽  
Ning‐Sheng Lai ◽  
...  
Keyword(s):  
Actin Cytoskeleton ◽  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
Identification And Characterization

Identification and characterization of AtI-2, an Arabidopsis homologue of an ancient protein phosphatase 1 (PP1) regulatory subunit

2011 ◽  
Vol 435 (1) ◽  
pp. 73-83 ◽  
Author(s):  
George W. Templeton ◽  
Mhairi Nimick ◽  
Nicholas Morrice ◽  
David Campbell ◽  
Marilyn Goudreault ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Biochemical Characterization ◽  
Affinity Purification ◽  
Bioinformatic Analysis ◽  
Protein Phosphatase 1 ◽  
Regulatory Subunit ◽  
Identification And Characterization ◽  
Eukaryotic Genomes

PP1 (protein phosphatase 1) is among the most conserved enzymes known, with one or more isoforms present in all sequenced eukaryotic genomes. PP1 dephosphorylates specific serine/threonine phosphoproteins as defined by associated regulatory or targeting subunits. In the present study we performed a PP1-binding screen to find putative PP1 interactors in Arabidopsis thaliana and uncovered a homologue of the ancient PP1 interactor, I-2 (inhibitor-2). Bioinformatic analysis revealed remarkable conservation of three regions of plant I-2 that play key roles in binding to PP1 and regulating its function. The sequence-related properties of plant I-2 were compared across eukaryotes, indicating a lack of I-2 in some species and the emergence points from key motifs during the evolution of this ancient regulator. Biochemical characterization of AtI-2 (Arabidopsis I-2) revealed its ability to inhibit all plant PP1 isoforms and inhibitory dependence requiring the primary interaction motif known as RVXF. Arabidopsis I-2 was shown to be a phosphoprotein in vivo that was enriched in the nucleus. TAP (tandem affinity purification)-tag experiments with plant I-2 showed in vivo association with several Arabidopsis PP1 isoforms and identified other potential I-2 binding proteins.

scholarly journals Identification and characterization of protein phosphatase 2C activation by ceramide

2012 ◽  
Vol 53 (8) ◽  
pp. 1513-1521 ◽  
Author(s):  
David M. Perry ◽  
Kazuyuki Kitatani ◽  
Patrick Roddy ◽  
Mohamad El-Osta ◽  
Yusuf A. Hannun
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 2C ◽  
Identification And Characterization
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