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each mutation in LRRK2 (show LRRK2 Proteins) and ARHGEF7 demonstrated its unique functional property, which may contribute to the pathogenesis of Parkinson disease
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 complex in health and disease
Data show association of G protein-coupled receptor (show ADRA1A Proteins) kinase-interacting protein (show CIB1 Proteins) 1 (GIT1), p21 (show CDKN1A Proteins)-activated kinase interacting exchange factor (betaPIX), and p21 protein (Cdc42/Rac)-activated kinase 1 (PAK1 (show PAK1 Proteins)) with centrosomes.
Data show the role of Rho guanine nucleotide exchange factor 7 (beta-PIX) to the regulation of high mobility of lung adenocarcinoma cell line H1299 via regulation of focal adhesions dynamics, changes in actin cytoskeleton organization and cell polarity.
Phosphorylation of LRRK2 (show LRRK2 Proteins) by casein kinase 1alpha regulates trans-Golgi clustering via differential interaction with ARHGEF7.
GIT1/betaPIX/Rac1/PAK pathway plays a crucial role in regulating GABA(A)R synaptic stability and hence inhibitory synaptic transmission with important implications for inhibitory plasticity and information processing in the brain.
Conversely, increased expression of betaPIX in breast cancer cell lines re-couples the Hippo kinase cassette to Yap (show YAP1 Proteins)/Taz (show TAZ Proteins), promoting localization of Yap (show YAP1 Proteins)/Taz (show TAZ Proteins) to the cytoplasm and inhibiting cell migration and proliferation.
Data indicate that suppression of c-Cbl (show CBL Proteins) protein by rho guanine nucleotide exchange factor 7 (Cool-1) may be critical for generation of at least a subset of glioblastoma (GBM).
The interaction of betaPix with srGAP1 (show SRGAP1 Proteins) is critical for maintaining suppressive crosstalk between Cdc42 (show CDC42 Proteins) and RhoA (show RHOA Proteins) during 3D collagen migration.
BetaPix phosphorylation at Ser (show SIGLEC1 Proteins)-340 upregulates Nox1 (show NOX1 Proteins) through Rac (show AKT1 Proteins) activation.
It provides for the first time, to our knowledge, a possible mechanism for the concerted action of tyrosine kinases, GIT1/betaPIX proteins, and Ca(2 (show CA2 Proteins)+) in the propagation of signals leading to the regulation of microtubule nucleation in activated mast cells.
beta-Pix controls the spatial localization of Rac1 activity to drive collective AVE migration at a critical stage in mouse development.
Therefore, we propose that PKCgamma (show PRKCG Proteins) positively modulates dopamine release through beta2PIX phosphorylation.
Glucose stimulates Cav-1 (show CAV1 Proteins) and induces its dissociation from Cdc42 (show CDC42 Proteins), to promote Cdc42 (show CDC42 Proteins)-betaPix binding and Cdc42 (show CDC42 Proteins) activation, and to trigger downstream signaling and ultimately sustain insulin (show INS Proteins) release.
a model by which SNX27 (show SNX27 Proteins) regulates trafficking of beta-Pix to focal adhesions and thereby influences cell motility.
betaPix-b(L) induced pinocytosis through cooperative action of the CH and Dbl (show MCF2 Proteins) homology (DH) domains, demonstrating the role of betaPix-b(L) in the regulation of membrane dynamics
Stat3 binds to betaPIX, a Rac1 activator,and regulates Rac1 activity to modulate the organization of actin cytoskeleton and directional migration
phosphorylation-dephosphorylation cycle of Cool-1 at Tyr (show TYR Proteins)-442 can serve as a key regulatory signal for focal complex assembly-disassembly, and consequently, for the migration and invasive activity of Src (show SRC Proteins)-transformed
P85 beta-PIX, located downstream of Rac1, is a key regulator for the activations of FAK (show PTK2 Proteins) or p38 MAP kinase (show MAPK14 Proteins) and plays a pivotal role in focal complex formation and cell motility.
Rho GTPases play a fundamental role in numerous cellular processes triggered by extracellular stimuli that work through G protein coupled receptors. The encoded protein belongs to a family of cytoplasmic proteins that activate the Ras-like family of Rho proteins by exchanging bound GDP for GTP. It forms a complex with the small GTP binding protein Rac1 and recruits Rac1 to membrane ruffles and to focal adhesions. This protein can induce membrane ruffling. Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene.
Rho guanine nucleotide exchange factor (GEF) 7
, Rho guanine nucleotide exchange factor 7
, rho guanine nucleotide exchange factor 7-like
, PAK-interacting exchange factor beta
, SH3 domain-containing proline-rich protein
, guanine nucleotide exchange factor 7
, rho guanine nucleotide exchange factor 7
, Pak interacting exchange factor
, Pak3 binding protein