C2 domain plays critical roles in localization of novel C2 domain-containing protein OsC2DP. [PDF]
Plant Signal Behav, 2019 OsC2DP is a cytosolic protein containing a C2 domain recently identified in rice, which is translocated to the plasma membrane in response to salt stress. Here, we further investigated the subcellular localization of OsC2DP by truncation analysis. In consistent with OsC2DP, OsC2DP1-165 containing C2 domain at the N-terminus was localized to the cytosol.
Fu S, Huang J, Chen Z, Xia J.
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The HRAS-binding C2 domain of PLCη2 suppresses tumor‐like synoviocytes and experimental arthritis in rheumatoid arthritis [PDF]
Experimental and Molecular MedicineFibroblast-like synoviocytes (FLSs), which are stromal cells that play key roles in rheumatoid arthritis (RA) pathophysiology, are characterized by a tumor-like phenotype and immunostimulatory actions.
Hyun Min Jeon +10 more
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BAIAP3, a C2 domain-containing Munc13 protein, controls the fate of dense-core vesicles in neuroendocrine cells. [PDF]
J Cell Biol, 2017 Dense-core vesicle (DCV) exocytosis is a SNARE (soluble N-ethylmaleimide–sensitive fusion attachment protein receptor)-dependent anterograde trafficking pathway that requires multiple proteins for regulation.
Zhang X +5 more
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Journal of Lipid Research, 2012 Group IVA cytosolic phospholipase A2 (cPLA2α) is an 85 kDa enzyme that regulates the release of arachidonic acid (AA) from the sn-2 position of membrane phospholipids.
Katherine E. Ward +3 more
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The 1.7 Å X-ray crystal structure of the porcine factor VIII C2 domain and binding analysis to anti-human C2 domain antibodies and phospholipid surfaces. [PDF]
PLoS ONE, 2015 The factor VIII C2 domain is essential for binding to activated platelet surfaces as well as the cofactor activity of factor VIII in blood coagulation. Inhibitory antibodies against the C2 domain commonly develop following factor VIII replacement therapy
Caileen M Brison +8 more
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Intramolecular C2 Domain-Mediated Autoinhibition of Protein Kinase C βII
Cell Reports, 2015 The signaling output of protein kinase C (PKC) is exquisitely controlled, with its disruption resulting in pathophysiologies. Identifying the structural basis for autoinhibition is central to developing effective therapies for cancer, where PKC activity ...
Corina E. Antal +4 more
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Membrane binding and lipid-protein interaction of the C2 domain from coagulation factor V [PDF]
Current Research in Structural BiologyAnchoring of coagulation factors to anionic regions of the membrane involves the C2 domain as a key player. The rate of enzymatic reactions of the coagulation factors is increased by several orders of magnitude upon membrane binding. However, the precise
Y. Zenmei Ohkubo +3 more
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The C2 domain augments Ras GTPase-activating protein catalytic activity. [PDF]
Proc Natl Acad Sci U S ARegulation of Ras GTPases by GTPase-activating proteins (GAPs) is essential for their normal signaling. Nine of the ten GAPs for Ras contain a C2 domain immediately proximal to their canonical GAP domain, and in RasGAP (p120GAP, p120RasGAP; RASA1 ) mutation of this domain is associated with ...
Paul ME +9 more
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Membrane-binding properties of the Factor VIII C2 domain. [PDF]
Biochemical Journal, 2011 Factor VIII functions as a cofactor for Factor IXa in a membrane-bound enzyme complex. Membrane binding accelerates the activity of the Factor VIIIa–Factor IXa complex approx. 100000-fold, and the major phospholipid-binding motif of Factor VIII is thought to be on the C2 domain.
V. Novakovic +5 more
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Frontiers in EndocrinologyIntroductionDouble C2-like domain beta (DOC2B) is a vesicle priming protein critical for glucose-stimulated insulin secretion in β-cells. Individuals with type 1 diabetes (T1D) have lower levels of DOC2B in their residual functional β-cell mass and ...
Diana Esparza +11 more
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