Results 21 to 30 of about 4,044,136 (204)
Regulation of inositol 5-phosphatase activity by the C2 domain of SHIP1 and SHIP2
bioRxiv, 2023 SHIP1, an inositol 5-phosphatase, plays a central role in cellular signalling. As such, it has been implicated in many conditions. Exploiting SHIP1 as a drug target will require structural knowledge and the design of selective small molecules.
W. Bradshaw +9 more
semanticscholar +1 more source
The Role of C2 Domains in Two Different Phosphatases: PTEN and SHIP2
Membranes, 2023 Phosphatase and tensin homologue (PTEN) and SH2-containing inositol 5′-phosphatase 2 (SHIP2) are structurally and functionally similar. They both consist of a phosphatase (Ptase) domain and an adjacent C2 domain, and both proteins dephosphorylate ...
Laura H. John +3 more
doaj +1 more source
A novel human TPIP splice-variant (TPIP-C2) mRNA, expressed in human and mouse tissues, strongly inhibits cell growth in HeLa cells. [PDF]
PLoS ONE, 2011 Alternative splicing of mRNAs is known to involve a major regulation of gene expression at RNA level in mammalian cells. The PTEN (Phosphatase and TENsin homologue deleted from the human chromosome 10), TPTE (Transmembrane Phosphatase with TEnsin ...
Rasmi Rekha Mishra +3 more
doaj +1 more source
Functions of Vertebrate Ferlins
Cells, 2020 Ferlins are multiple-C2-domain proteins involved in Ca2+-triggered membrane dynamics within the secretory, endocytic and lysosomal pathways. In bony vertebrates there are six ferlin genes encoding, in humans, dysferlin, otoferlin, myoferlin, Fer1L5 and 6
Anna V. Bulankina, Sven Thoms
doaj +1 more source
European Journal of Cell Biology, 2023 Many signaling processes rely on information decoding at the plasma membrane, and membrane-associated proteins and their complexes are fundamental for regulating this process.
Mingming Cui +2 more
doaj +1 more source
Superdiffusive motion of membrane-targeting C2 domains [PDF]
Scientific Reports, 2015 AbstractMembrane-targeting domains play crucial roles in the recruitment of signalling molecules to the plasma membrane. For most peripheral proteins, the protein-to-membrane interaction is transient. After proteins dissociate from the membrane they have been observed to rebind following brief excursions in the bulk solution.
Grace Campagnola +4 more
openaire +3 more sources
Lipid binding domains: more than simple lipid effectors
Journal of Lipid Research, 2009 The spatial and temporal regulation of lipid molecules in cell membranes is a hallmark of cellular signaling and membrane trafficking events. Lipid-mediated targeting provides for strict control and versatility, because cell membranes harbor a large ...
Robert V. Stahelin
doaj +1 more source
Crossover between different regimes of inhomogeneous superconductivity in planar superconductor-ferromagnet hybrids [PDF]
, 2011 We studied experimentally the effect of a stripe-like domain structure in a ferromagnetic BaFe_{12}O_{19} substrate on the magnetoresistance of a superconducting Pb microbridge.
Aladyshkin, A. Yu. +7 more
core +3 more sources
The C2 Domain of PKCδ Is a Phosphotyrosine Binding Domain [PDF]
Cell, 2005 In eukaryotic cells, the SH2 and PTB domains mediate protein-protein interactions by recognizing phosphotyrosine residues on target proteins. Here we make the unexpected finding that the C2 domain of PKCdelta directly binds to phosphotyrosine peptides in a sequence-specific manner. We provide evidence that this domain mediates PKCdelta interaction with
Benes, Cyril H. +5 more
openaire +2 more sources
μ-calpain binds to lipid bilayers via the exposed hydrophobic surface of its Ca2+-activated conformation [PDF]
, 2006 μ- and m-calpain are cysteine proteases requiring micro- and millimolar Ca2+ concentrations for their activation in vitro. Among other mechanisms, interaction of calpains with membrane phospholipids has been proposed to facilitate their activation by ...
Assfalg-Machleidt, Irmgard +5 more
core +4 more sources