Transmembrane Receptors and Channels by A.G. Lee (Eds.)

By A.G. Lee (Eds.)

Quantity 6 of Biomembranes covers transmembrane receptors and channels. a very vital function for the membrane is that of passing messages among a mobilephone and its setting. half I of this quantity covers receptors for hormones and progress components. the following, as in such a lot of different parts of mobile biology, the appliance of the tools of molecular biology have ended in the popularity of a few households of receptors. in most cases, such receptors comprise an extracellular ligand binding area, a transmembrane area, and an intracellular catalytic area whose activation, because of ligand binding, results in new release of moment messengers in the mobilephone and stimulation of more than a few cytosolic enzymes. an alternate signaling method, exploited particularly within the anxious process, is to exploit ion channels to permit managed circulate of monovalent (Na+, K+) or divalent (Ca2+) cations in or out of the telephone, leading to alterations in membrane strength or adjustments within the intracellular focus of Ca2+. half II of this quantity is anxious with those ion channels and with different, frequently easier, ion channel structures whose learn can throw mild on channel mechanism.

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Lesser degrees of phosphorylation within this motif can result in reduced activity. Both chains are encoded by a single gene and the mature product is produced by proteolytic cleavage at a Arg-Arg-Lys-Arg sequence. All three receptors are closely related to one another throughout their entire length, except in their extreme C-termini. The C-terminal tail of IRR (at 57 or 60 residues) is considerably shorter than that of either the IR (98 residues) or the IGF-IR (107 residues). Despite containing a number of autophosphorylation sites, the tail appears dispensable for signaling.

1993). Despite the high degree of structural similarity, c-^r^B-2 does not bind any of the known EGFR ligands. , 1988). This occurs by transphosphorylation by the activated EGFR and it has been suggested that this indirect phosphorylation and activation of c-erbB-2 by EGF may represent a receptor PTK phosphorylation cascade (Connelly and Stem, 1990). , 1992). A number of putative ligands for c-^r^B-2 have been identified, but the precise nature of these factors remains a point of intense study.

This receptor is virtually ubiquitously expressed, although the actual receptor number in different cell populations can vary from less than 100 per cell in erythrocytes to greater than 200,000 in adipocytes and hepatocytes (reviewed in Tavare and Siddle, 1993). , 1986) and the insulinrelated receptor (IRR; Shier and Watt, 1989; Zhang and Roth, 1992). The IR and IGF-IR exhibit the highest degree of similarity among the ectodomains of PTKs and have been found to share partial ligand specificity.

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