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our work identifies DOCK5 as a key regulator of epithelial invasion and metastasis, and demonstrates that suppression of DOCK5 by GIT2 represents a previously unappreciated mechanism for coordination of Rho and Rac (show AKT1 Proteins) GTPases.
we discuss recent findings in key physiological systems that exemplify current understanding of the function of this important regulatory complex. Further, we draw attention to gaps in crucial information that remain to be filled to allow a better understanding of the many roles of the GIT-PIX (show ARHGEF7 Proteins) complex in health and disease
Short-term EGF (show EGF Proteins) stimulation if of lung tumor cells can increase the interaction between RUSC2 and GIT2, prolonged stimulation leads to a decrease of their interaction through activating Rab35 (show RAB35 Proteins).
GIT2 plays an important role in MRE11/ATM/H2AX-mediated DNA damage responses.
ADMA and L-arginine (show GATM Proteins) are substrates of human CAT2A, CAT2B, OCT2 and MATE1. Transport kinetics of CAT2A, CAT2B, and OCT2 indicate a low affinity, high capacity transport, which may be relevant for renal and hepatic elimination of ADMA or L-arginine (show GATM Proteins)
Zeb1 is regulated by the Arf GTPase-activating protein (GAP) Git2.
GIT2 protein is tightly associated with PIX (show ARHGEF7 Proteins) family Rac1/Cdc42 (show CDC42 Proteins) guanine nucleotide exchange factors as a multimeric nexus capable of linking together important signaling molecules.
The expression level of lymphocyte GRK (show GRK4 Proteins) might show the severity of CHF, and ACEI treatment could reduce the level of GRK (show GRK4 Proteins) in CHF patients.
GTI proteins regulate cytoskeletal dynamics by feedback inhibition of Rac1, they participate in receptor internalization by regulating membrane trafficking between
These results suggest that inactivation of GIT2 function is a required step for induction of cell motility and that GIT2 may be a target of oncogenic signaling pathways that regulate cell migration.
The cell adhesion-associated protein Git2 regulates morphogenetic movements during zebrafish embryonic development.
GIT2(-/-) mice present a prematurely distorted thymic structure and dysfunction compared to age-matched 12 month-old wild-type control (C57BL/6) mice.
GIT2 is an essential terminator of TLR signaling and loss of GIT2 leads to uncontrolled inflammation and severe organ damage
these findings underscore the importance of the cytoskeleton in both osteoblast and osteoclast function and demonstrate that GIT2 plays essential roles in skeletal metabolism, affecting both bone formation and bone resorption in vivo.
GIT2 has a key role in regulating the chemokine (show CCL1 Proteins)-mediated motility of double-positive thymocytes
Results suggest that paxillin (show PXN Proteins)-kinase-linker is an integral component of growth factor and cell adhesion cross-talk signaling, controlling the development of front-rear cell polarity and directional cell migration.
GIT2 links chemotaxis and superoxide production in neutrophils.Loss of GIT2 in vivo leads to an immunodeficient state.
Analysis of endogenous GIT expression revealed a nearly ubiquitous distribution of GIT2, whereas GIT1 is restricted to specific cell types even in tissues with apparently high GIT1 expression and is entirely absent from some tissues.
Hence, GIT2-KO mice display anxiety-like behavior in an absence of depressive-like responses.
xGit2 and xRhoGAP 11A regulate convergent extension and tissue separation in Xenopus gastrulation
This gene encodes a member of the GIT protein family, which interact with G protein-coupled receptor kinases and possess ADP-ribosylation factor (ARF) GTPase-activating protein (GAP) activity. GIT proteins traffic between cytoplasmic complexes, focal adhesions, and the cell periphery, and interact with Pak interacting exchange factor beta (PIX) to form large oligomeric complexes that transiently recruit other proteins. GIT proteins regulate cytoskeletal dynamics and participate in receptor internalization and membrane trafficking. This gene has been shown to repress lamellipodial extension and focal adhesion turnover, and is thought to regulate cell motility. This gene undergoes extensive alternative splicing to generate multiple isoforms, but the full-length nature of some of these variants has not been determined. The various isoforms have functional differences, with respect to ARF GAP activity and to G protein-coupled receptor kinase 2 binding.
ARF GAP GIT2
, ARF GTPase-activating protein GIT2
, G protein-coupled receptor kinase-interactor 2
, GRK-interacting protein 2
, cool-associated, tyrosine phosphorylated protein 2
, cool-interacting tyrosine-phosphorylated protein 2
, G protein-coupled receptor kinase interactor 2
, ARF GTPase activating protein 2
, cool associated tyrosine phosphorylated-2
, G protein-coupled receptor kinase interacting ArfGAP 2 L homeolog