GTPase


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GTPase

[′jē‚tē¦pās]
(cell and molecular biology)
One of a family of monomeric GTP-binding proteins.
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The signaling activity of the disassociated G protein ends when the GTP associated with G[alpha] is degraded to GDP (often by the G[alpha] subunit's own GTPase activity) and the G[alpha] subunit recombines with a G[beta][gamma] dimer to form a new heterotrimer, which can then bind to the intracellular domain of the transmembrane receptor.
APP and its [sz]-C-terminal-fragment ([sz]-CTF) can activate Rab5, a Rab-family GTPase located in early endosomes.
Based on this analysis, in addition to 7 transmembrane domains, extra-territorial, from the 4-266 amino acid residues may be a HTTM (Horizontally Transferred Transmembrane Domain) region; the 9-168 amino acid residues be acid phosphatase protein family function domain; the 85-285 amino acid residues be a GTPase activated TBC domain; the 105-290 amino acid residues be structural domain similar to TRAM receptor (Fig.
33) Classical dynamins contain a GTPase domain, middle domain, pleckstrin-homology (PH) domain, GTPase effector doman (GED) and proline-rich domain.
Other groups that were significantly upregulated and enriched were "Small GTPase superfamily," from 240-300 min, and "GTPase-mediated signal transduction," at 270 min.
Its approach to gene therapy uses a viral vector known as adeno-associated virus (AAV), which delivers a codon-optimised copy of the retinitis pigmentosa GTPase regulator (RPGR) gene into cells of the eye.
IFT27, encoding a small GTPase component of IFT particles, is mutated in a consanguineous family with Bardet-Biedl syndrome.
12) These mutations result in a decreased GTPase activity, locking the protein in its active, GTP-bound state.
A core complex of BBS proteins cooperates with the GTPase Rab8 to promote ciliary membrane biogenesis.
Its activating mutations abolish the intrinsic GTPase activity, resulting in constitutively active KRAS proteins that activate downstream signaling pathways and can lead to carcinogenesis.