Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Identification of two tyrosine residues required for the intramolecular mechanism implicated in GIT1 activation.

PloS one - 1 Jan 2014

Totaro Antonio, Astro Veronica, Tonoli Diletta, de Curtis Ivan

Abstract excerpt

GIT1 is an ArfGAP and scaffolding protein regulating cell adhesion and migration. The multidomain structure of GIT1 allows the interaction with several partners. Binding of GIT1 to some of its partners requires activation of the GIT1 polypeptide. Our previous studies indicated that binding of paxillin to GIT1 is enhanced by release of an intramolecular interaction between the amino-terminal and carboxy-terminal...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adaptor Proteins, Signal Transducing
Share to Cell Adhesion

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cell Movement

Share to Chlorocebus aethiops

Share to COS Cells

Share to Paxillin

Share to Tyrosine

Share to Wound Healing

Source

Open in PubMed Open full text

Identifiers

PMID: 24699139
DOI: 10.1371/journal.pone.0093199
PMCID: PMC3974724

Genes

GIT1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of two tyrosine residues required for the intramolecular mechanism implicated in GIT1 activation.PMID 24699139Read ↗

Identification of an intramolecular interaction important for the regulation of GIT1 functions.Semantic proximity Read ↗

GIT1 activates p21-activated kinase through a mechanism independent of p21 binding.Semantic proximity Read ↗

Receptor tyrosine kinases activate heterotrimeric G proteins via phosphorylation within the interdomain cleft of GαiSemantic proximity Read ↗

GIT1 is a scaffold for ERK1/2 activation in focal adhesions.Semantic proximity Read ↗

The GTPase-activating protein Rap1GAP uses a catalytic asparagine.Semantic proximity Read ↗

Mutational analysis reveals a single binding interface between RhoA and its effector, PRK1.Semantic proximity Read ↗

Calcium and calmodulin-dependent serine/threonine protein kinase type II (CaMKII)-mediated intramolecular opening of integrin cytoplasmic domain-associated protein-1 (ICAP-1α) negatively regulates β1 integrins.Semantic proximity Read ↗

An activating mutant of Rac1 that fails to interact with Rho GDP-dissociation inhibitor stimulates membrane ruffling in mammalian cells.Semantic proximity Read ↗

Protein kinase A-dependent phosphorylation of Rap1 regulates its membrane localization and cell migration.Semantic proximity Read ↗

Galpha12 regulates protein interactions within the MDCK cell tight junction and inhibits tight-junction assembly.Semantic proximity Read ↗

RACK1 binds to a signal transfer region of G betagamma and inhibits phospholipase C beta2 activation.Semantic proximity Read ↗

Synapse formation is regulated by the signaling adaptor GIT1.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.