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CLEC4C is a membrane protein of plasmacytoid dendritic cells, which is used as a marker for this kind of cells and denoted as CD303 in the nomenclature of the Cluster of differentiation.
The latter interaction leads to receptor activation, and the transduction of the ligand binding signal across the cell plasma membrane to the cytoplasmic G protein GNAI2.
The TRPV4 (transient receptor potential vanilloid 4) gene, located on chromosome 12, encodes for a protein that serves as an ion channel, typically found in the plasma membrane and is permeable to Ca2+.
The C-terminal DHR2 domain functions as an atypical GEF domain for small G proteins (see Dock180: structure and function) and the DHR1 domain is known, in some DOCK-A/B/C subfamily proteins, to be involved in their recruitment to the plasma membrane.
Transmembrane protein which may be responsible for uptake and transport of tunicamycin at the plasma membrane.
CD36 and scavenger receptor class BI (SR-BI) are identified as oxidized LDL receptors and classified into class B. Both proteins have two transmembrane domains, and they are concentrated in a specific plasma membrane microdomain, the caveolae.
The AVPR1A is endocytosed by binding to beta arrestin, which dissociates rapidly from AVPR1A to allow it to return to the plasma membrane; however, upon activation, AVPR1A can heterodimerize with AVPR2 to increase beta-arrestin-mediated endocytosis (and intracellular accumulation) of AVPR1A, since AVPR2 is far less likely to dissociate from beta-arrestin.
V-ATPase 116 kDa isoform a2 is a subunit of the vacuolar ATPase (v-ATPase), an heteromultimeric enzyme that is present in intracellular vesicles and in the plasma membrane of specialized cells, and which is essential for the acidification of diverse cellular components.
When lipid diacylglycerol (DAG) binds to the C1 domain, CHN1 is transferred to the plasma membrane and negatively regulates Rho-family small GTPases RAC1 and CDC42, thus causing the morphological change of axons by pruning the ends of axon dendrites.
LDL in the blood binds to LDL receptors on the surface of fibroblasts; these receptors concentrate in coated pits (they are about 200x as concentrated here as along the rest of the cell’s plasma membrane) and are internalised when the pit becomes a coated vesicle.
This gene encodes a highly conserved protein consisting entirely of PLAT (polycystin/lipoxygenase/alpha-toxin) domains, thought to be involved in targeting proteins to the plasma membrane.
In the enterocyte microvillus, the structural core is attached to the plasma membrane along its length by lateral arms made of myosin 1a and Ca2+ binding protein calmodulin.
In the mouse (the best characterised mammalian system), the zona glycoprotein, ZP3, is responsible for sperm binding, adhering to proteins on the sperm plasma membrane (GalT).