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- W1985643113 abstract "•IQGAP proteins scaffold diverse signaling molecules. •IQGAPs mediate crosstalk between signaling pathways. •IQGAP1 regulates nuclear processes, including transcription. Since its discovery in 1994, recognized cellular functions for the scaffold protein IQGAP1 have expanded immensely. Over 100 unique IQGAP1-interacting proteins have been identified, implicating IQGAP1 as a critical integrator of cellular signaling pathways. Initial research established functions for IQGAP1 in cell–cell adhesion, cell migration, and cell signaling. Recent studies have revealed additional IQGAP1 binding partners, expanding the biological roles of IQGAP1. These include crosstalk between signaling cascades, regulation of nuclear function, and Wnt pathway potentiation. Investigation of the IQGAP2 and IQGAP3 homologs demonstrates unique functions, some of which differ from those of IQGAP1. Summarized here are recent observations that enhance our understanding of IQGAP proteins in the integration of diverse signaling pathways. Since its discovery in 1994, recognized cellular functions for the scaffold protein IQGAP1 have expanded immensely. Over 100 unique IQGAP1-interacting proteins have been identified, implicating IQGAP1 as a critical integrator of cellular signaling pathways. Initial research established functions for IQGAP1 in cell–cell adhesion, cell migration, and cell signaling. Recent studies have revealed additional IQGAP1 binding partners, expanding the biological roles of IQGAP1. These include crosstalk between signaling cascades, regulation of nuclear function, and Wnt pathway potentiation. Investigation of the IQGAP2 and IQGAP3 homologs demonstrates unique functions, some of which differ from those of IQGAP1. Summarized here are recent observations that enhance our understanding of IQGAP proteins in the integration of diverse signaling pathways. forms a destruction complex with axin, CK1, DYRK, and GSK3β. The APC destruction complex phosphorylates β-catenin to mark it for ubiquitination and degradation, thereby inhibiting canonical Wnt signaling. APC can also coordinate actin and microtubule dynamics during cell migration through interactions with β-catenin and E-cadherin. a large family of proteins that are targeted to specific cellular locations and form signaling complexes that contain PKA and other signaling molecules. a kinase activated by PtdInsP3 binding and Akt phosphorylation. Akt phosphorylates substrates to regulate cellular processes including cell survival and proliferation. a domain that interacts with F-actin. a cytoplasmic protein that binds to Fzd on Wnt–Fzd stimulation. Dvl inhibits GSK3β activity and allows for the nuclear translocation of β-catenin and activation of canonical Wnt signaling. complexes of proteins that attach to ECM proteins and interact with the cytoskeleton. a domain similar to the RasGAP catalytic domain. a family of 7-transmembrane receptors that transduce signals from various inputs. Typically, GPCRs are associated with heterotrimeric Gα and Gβ/Gγ G proteins. Ligand binding results in Gα regulation of enzymes to alter the concentrations of second messengers such as cAMP, IP3, DAG, and Ca2+. proteins that inactivate small GTPases by enhancing their intrinsic GTPase activity, which hydrolyzes GTP to GDP. protein that catalyzes the release of GDP from inactive small GTPases. This enables GTP, which is in excess in the cell, to bind to the GTPase. sequences containing Iso/Leu and Gln residues that are often found in multiple motifs within selected proteins. IQ motifs mediate interactions with Ca2+-binding proteins, including calmodulin and S100 family proteins. proteins that bind to the growing (plus) end of microtubules, connecting them to subcellular locations necessary for processes like migration and cytokinesis. Examples include EB1 and CLASP2. the MAPK pathway involves the sequential activation of multiple kinases to activate ERK, which regulates processes like cell differentiation and proliferation. binds the Arp2/3 complex to promote actin branching. lincRNAs lack open reading frames yet have important roles in the control of gene expression; includes NRON. a family of small GTPases that are activated downstream of receptors to regulate the activity of kinases/other signaling proteins in signaling pathways. a domain that is unique to IQGAP proteins. a family of proteins that mediate signal transduction from extracellular signaling molecules to initiate intracellular signaling pathways. Ligand activation of RTK usually results in receptor dimerization and autophosphorylation, with subsequent phosphorylation of substrates on tyrosine residues, and assembly of signaling adaptors on phosphorylated tyrosines. DNA-binding proteins that target specific regulatory sequences to control gene expression. a structure that assembles on the endoplasmic reticulum near the midpoint of the trailing edge of migrating cells. It assembles multiple proteins required for cell retraction to promote cleavage of proteins by calpain and retraction by myosin along actin filaments. a tryptophan-containing domain that in most proteins interacts with proline-rich regions." @default.
- W1985643113 created "2016-06-24" @default.
- W1985643113 creator A5015223159 @default.
- W1985643113 creator A5017586422 @default.
- W1985643113 creator A5028231801 @default.
- W1985643113 date "2015-03-01" @default.
- W1985643113 modified "2023-10-12" @default.
- W1985643113 title "IQGAPs choreograph cellular signaling from the membrane to the nucleus" @default.
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