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Rnd Protein
Rnd is a subclass of the Rho family of GTPases and includes: *Rnd1 *Rnd2 *Rnd3 (also called RhoE) Functions include downregulation of stress fibres and focal adhesions. See also *Rho family of GTPases The Rho family of GTPases is a family of small (~21 kDa) signaling G proteins, and is a subfamily of the Ras superfamily. The members of the Rho GTPase family have been shown to regulate many aspects of intracellular actin dynamics, and are found ... References EC 3.6.5 {{3.6-enzyme-stub ...
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GTPase
GTPases are a large family of hydrolase enzymes that bind to the nucleotide guanosine triphosphate (GTP) and hydrolyze it to guanosine diphosphate (GDP). The GTP binding and hydrolysis takes place in the highly conserved P-loop "G domain", a protein domain common to many GTPases. Functions GTPases function as molecular switches or timers in many fundamental cellular processes. Examples of these roles include: * Signal transduction in response to activation of cell surface receptors, including transmembrane receptors such as those mediating taste, smell and vision. * Protein biosynthesis (a.k.a. translation) at the ribosome. * Regulation of cell differentiation, proliferation, division and movement. * Translocation of proteins through membranes. * Transport of vesicles within the cell, and vesicle-mediated secretion and uptake, through GTPase control of vesicle coat assembly. GTPases are active when bound to GTP and inactive when bound to GDP. In the generalized recepto ...
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Rnd1
Rnd1 is a small (~21 kDa) signaling G protein (to be specific, a GTPase), and is a member of the Rnd subgroup of the Rho family of GTPases. It is encoded by the gene RND1. It contributes to regulating the organization of the actin cytoskeleton in response to extracellular growth factors (Nobes et al., 1998). upplied by OMIMref name="entrez" /> Interactions Rnd1 has been shown to interact with GRB7, PLXNB1, PDE6D, ARHGAP5 Rho GTPase-activating protein 5 is an enzyme that in humans is encoded by the ''ARHGAP5'' gene. Function Rho GTPase activating protein 5 negatively regulates RHO GTPases, a family that may mediate cytoskeleton changes by stimulating the hydrol ... and UBXD5. References Further reading

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Rnd2
Rnd2 is a small (~21 kDa) signaling G protein (to be specific, a GTPase), and is a member of the Rnd subgroup of the Rho family of GTPases. It is encoded by the gene RND2. Function It contributes to regulating the organization of the actin cytoskeleton in response to extracellular growth factors (Nobes et al., 1998). upplied by OMIMref name="entrez2"> This particular family member has been implicated in the regulation of neuronal morphology and endosomal trafficking. Clinical significance The gene localizes to chromosome 17 and is the centromeric neighbor of the breast-ovarian cancer susceptibility gene BRCA1. Interactions Rnd2 has been shown to interact with: * ARHGAP5 Rho GTPase-activating protein 5 is an enzyme that in humans is encoded by the ''ARHGAP5'' gene. Function Rho GTPase activating protein 5 negatively regulates RHO GTPases, a family that may mediate cytoskeleton changes by stimulating the hydrol ..., * RACGAP1, and * UBXD5. References Furt ...
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Rnd3
Rnd3 is a small (~21 kDa) signaling G protein (to be specific, a GTPase), and is a member of the Rnd subgroup of the Rho family of GTPases. It is encoded by the gene RND3. Like other members of the Rho family of Ras-related GTPases it regulates the organization of the actin cytoskeleton in response to extracellular growth factors. Regulation Most Rho family members cycle between an inactive GDP-bound form and an active GTP-bound form. However, members of the Rnd subgroup of the Rho family are exceptions to this, binding detectably only to GTP, while having low GTPase activity, if any. Instead, Rnd family proteins are regulated through other mechanisms that control their production, degradation, phosphorylation, and localization. Interactions In its GTP-bound form, RhoA exposes regions that allow it to interact with downstream targets. Rnd3 contains a region which is similar to the one RhoA exposes for interaction with ROCK1, allowing Rnd3 to compete with RhoA for interac ...
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Stress Fibre
Stress fibers are contractile actin bundles found in non-muscle cells. They are composed of actin (microfilaments) and non-muscle myosin II (NMMII), and also contain various crosslinking proteins, such as α-actinin, to form a highly regulated actomyosin structure within non-muscle cells. Stress fibers have been shown to play an important role in cellular contractility, providing force for a number of functions such as cell adhesion, migration and morphogenesis. Structure Stress fibers are primarily composed of actin and myosin. Actin is a ~43kDa globular protein, and can polymerize to form long filamentous structures. These filaments are made of two strands of actin monomers (or protofilaments) wrapping around each other, to create a single actin filament. Because actin monomers are not symmetrical molecules, their filaments have polarity based upon the structure of the actin monomer, which will allow one end of the actin filament to polymerize faster than the other. The end ...
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Focal Adhesion
In cell biology, focal adhesions (also cell–matrix adhesions or FAs) are large macromolecular assemblies through which mechanical force and regulatory signals are transmitted between the extracellular matrix (ECM) and an interacting cell. More precisely, focal adhesions are the sub-cellular structures that mediate the regulatory effects (i.e., signaling events) of a cell in response to ECM adhesion. Focal adhesions serve as the mechanical linkages to the ECM, and as a biochemical signaling hub to concentrate and direct numerous signaling proteins at sites of integrin binding and clustering. Structure and function Focal adhesions are integrin-containing, multi-protein structures that form mechanical links between intracellular actin bundles and the extracellular substrate in many cell types. Focal adhesions are large, dynamic protein complexes through which the cytoskeleton of a cell connects to the ECM. They are limited to clearly defined ranges of the cell, at which the pla ...
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Rho Family Of GTPases
The Rho family of GTPases is a family of small (~21 kDa) signaling G proteins, and is a subfamily of the Ras superfamily. The members of the Rho GTPase family have been shown to regulate many aspects of intracellular actin dynamics, and are found in all eukaryotic kingdoms, including yeasts and some plants. Three members of the family have been studied in detail: Cdc42, Rac1, and RhoA. All G proteins are "molecular switches", and Rho proteins play a role in organelle development, cytoskeletal dynamics, cell movement, and other common cellular functions. History Identification of the Rho family of GTPases began in the mid-1980s. The first identified Rho member was RhoA, isolated serendipitously in 1985 from a low stringency cDNA screening. Rac1 and Rac2 were identified next, in 1989 followed by Cdc42 in 1990. Eight additional mammalian Rho members were identified from biological screenings until the late 1990s, a turning point in biology where availability of complete genome seq ...
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