Results 71 to 80 of about 2,399,730 (304)

Protein Kinases and Phosphatases of the Plastid and Their Potential Role in Starch Metabolism

Frontiers in Plant Science, 2018
Phospho-proteomic studies have confirmed that phosphorylation is a common mechanism to regulate protein function in the chloroplast, including the enzymes of starch metabolism.
Chris White-Gloria, Jayde J. Johnson, Kayla Marritt, Amr Kataya, Amr Kataya, Ahmad Vahab, Greg B. Moorhead   +6 more
doaj   +1 more source

SHIP2 inhibition alters redox‐induced PI3K/AKT and MAP kinase pathways via PTEN over‐activation in cervical cancer cells

FEBS Open Bio, 2020
Phosphatidylinositol (3,4,5)‐trisphosphate (PI(3,4,5)P3) is required for protein kinase B (AKT) activation. The level of PI(3,4,5)P3 is constantly regulated through balanced synthesis by phosphoinositide 3‐kinase (PI3K) and degradation by ...
Abdelhalim Azzi
doaj   +1 more source

Septin 9 PB domains coordinate centrosome positioning and microtubule acetylation to control epithelial polarity

FEBS Letters, EarlyView.
Septin 9 polybasic domains couple phosphoinositide‐rich membrane binding to centrosome positioning, Golgi organization, and microtubule acetylation to control epithelial polarity. Their loss disrupts this axis, causing centrosome mispositioning, Golgi fragmentation, reduced microtubule acetylation, and polarity inversion via upregulation of the ...
Ting ting Cai, Mohyeddine Omrane, Nassima Benzoubir, Didier Samuel, Ama Gassama‐Diagne   +4 more
wiley   +1 more source

Effects of light and the regulatory Beta subunit composition of protein phosphatase 2A on the susceptibility of Arabidopsis thaliana to aphid (Myzus persicae) infestation

Frontiers in Plant Science, 2014
The interactions between biotic and abiotic stress signalling pathways are complex and poorly understood but protein kinase/phosphatase cascades are potentially important components.
Brwa eRasool, Barbara eKarpinska, Grzegorz eKonert, Guido eDurian, Konstantin eDenessiouk, Saijaliisa eKangasjärvi, Christine Helen Foyer   +6 more
doaj   +1 more source

Phosphoinositides and inositol phosphates as molecular glues

FEBS Letters, EarlyView.
Inositol phosphates (IPs) and phosphoinositides (PIPs) regulate diverse eukaryotic processes. Beyond recruiting signaling proteins or acting as structural cofactors, recent studies suggest they mediate protein–protein interactions as natural molecular glues.
Aleshia Seaton‐Terry, Alexander J. Cutright, Mong Na Claire Loi, Jessica Martin, Joseph W. Gilligan, Jakub N. Kubina, Michael J. Arambula, Susanna Tanada Palmu, Daniella Zhou, Raymond D. Blind   +9 more
wiley   +1 more source

Deletion of Protein Tyrosine Phosphatase Nonreceptor Type 2 in Intestinal Epithelial Cells Results in Upregulation of the Related Phosphatase Protein Tyrosine Phosphatase Nonreceptor Type 23 [PDF]

Inflammatory Intestinal Diseases, 2019
<b><i>Background/Aims:</i></b> Knockdown of protein tyrosine phosphatase nonreceptor type 2 (<i>PTPN2</i>) exaggerates IFN-γ-induced intestinal barrier defects, but mice constitutively lacking <i>PTPN2</i> in epithelial cells (PTPN2xVilCre mice) do not show changes in epithelial function or enhanced ...
Ulugöl, Sima, Hering, Larissa, Manzini, Roberto, Montalban Arques, Ana, Gottier, Claudia, Lang, Silvia, Scharl, Michael, Spalinger, Marianne R   +7 more
openaire   +3 more sources

Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates

FEBS Letters, EarlyView.
Inositol pyrophosphates are energy‐rich signaling molecules that perform critical functions in cells. Three different families of phosphatases hydrolyze the β phosphate of the inositol pyrophosphate molecules: two have narrow specificities and one is promiscuous.
Ronda J. Rolfes
wiley   +1 more source

ABL kinase‐dependent phosphorylation of SH proteins promotes their direct interaction with CRK family SH2 domains

FEBS Letters, EarlyView.
CT10 regulator of kinase (CRK) and CRK‐Like (CRKL) are signaling adaptors driving cell adhesion, motility, differentiation, and proliferation. SH2‐domain containing (SH) proteins are enriched in YXXP motifs which when phosphorylated create preferred binding sites for CRK family SH2 domains.
Phoebe M. Cousens, Brendan W. Chandler, Anna M. Schmoker, Jaye L. Weinert, Charlotte A. Kearns, Warren T. Yacawych, Amila Šemić, Alicia M. Ebert, Bryan A. Ballif   +8 more
wiley   +1 more source

Domains of phosphatase inhibitor-2 involved in the control of the ATP-Mg-dependent protein phosphatase.

Journal of Biological Chemistry, 1994
Inhibitor-2 (I-2) inhibits the free catalytic subunit of type 1 phosphatase (CS1) and controls the cyclic inactivation/activation of CS1 in the ATP-Mg-dependent protein phosphatase complex. We report here the effect of mutations on these two properties of I-2.
I K, Park, A A, DePaoli-Roach
openaire   +2 more sources

Characterization of the Inhibition of Protein Phosphatase-1 by DARPP-32 and Inhibitor-2 [PDF]

Journal of Biological Chemistry, 1999
Phospho-DARPP-32 (where DARPP-32 is dopamine- and cAMP-regulated phosphoprotein, Mr 32,000), its homolog, phospho-inhibitor-1, and inhibitor-2 are potent inhibitors (IC50 approximately 1 nM) of the catalytic subunit of protein phosphatase-1 (PP1). Our previous studies have indicated that a region encompassing residues 6-11 (RKKIQF) and phospho-Thr-34 ...
H B, Huang, A, Horiuchi, T, Watanabe, S R, Shih, H J, Tsay, H C, Li, P, Greengard, A C, Nairn   +7 more
openaire   +2 more sources