docking protein

Docking protein 4 is a protein that in humans is encoded by the DOK4 gene.

GAB proteins were one of the first docking proteins identified in the mammalian signal transduction pathway.

LMDs are docking proteins which function as platforms mediating interaction between different signaling pathways and assisting with signal integration.

Docking proteins such as GRB2 contains an SH2 domain that binds to the phosphotyrosine residues of the activated receptor.

GAB2 is a docking protein with a conserved, folded PH domain attached to the membrane and a large disordered region, which hosts interactions with signaling molecules.

In this pathway, recruitment of a guanine nucleotide exchange factor by the adaptor and docking proteins leads to activation of a membrane-associated G-protein known as Ras.

GAB2 along with many other adaptor, scaffold, and docking proteins, was discovered in the mid 1990s during the isolation and cloning of protein tyrosine kinase substrates and association partners.

Signal recognition particle (SRP) receptor, also called docking protein, is a dimer composed of 2 different subunits that are associated exclusively with the rough ER in mammalian cells.

GAB2 is a large multi-site docking protein (LMD) of about 100kD which has a folded N-terminal domain attached to an extended, disordered C-terminal tail rich in short linear motifs.

Moreover, incubation of the TGFβ 1 sensitive carcinoma cells with TGFβ 1 caused immobilization of the docking protein p130 casand of the guanine nucleotide exchange factor SOS to the cytoskeleton.

When overexpressed in cultured cells, these mutant GTPases function as dominant-suppressors of their endogenous counterparts [ 26 27 31 ] , presumably because they can compete for interaction with effectors, exchange factors or docking proteins, but cannot cycle on and off membranes in a nucleotide-dependent manner.