Rap1GTPtä

Rap1GTPtä is not a widely recognized distinct protein name in major biological databases. It most likely denotes the GTP-bound, active form of Rap1, a small GTPase in the Ras superfamily.

Rap1 proteins function as molecular switches in cells, cycling between inactive GDP-bound and active GTP-bound states. Activation is driven by guanine nucleotide exchange factors (GEFs), which promote GDP release and GTP binding; inactivation is mediated by GTPase-activating proteins (GAPs) that accelerate GTP hydrolysis.

Rap1 is typically localized to the plasma membrane and other membranes, aided by lipid post-translational modifications; this localization enables interactions with a range of effector proteins that regulate adhesion, polarity, and junctional dynamics.

Physiological roles: in mammals, Rap1 signaling influences cell–cell adhesion by regulating cadherins and integrins, modulates endothelial barrier function, and participates in leukocyte trafficking and synaptic organization, with effects that depend on cell type and context.

Genetics: In humans, RAP1A and RAP1B genes encode Rap1 proteins. The activity state is determined by the balance of GEFs and GAPs and by downstream signaling networks. The GTP-bound form, Rap1GTP, transmits signals to multiple effectors that mediate changes in the actin cytoskeleton and adhesion machinery.

Note: If encountered in literature as Rap1GTPtä, it should be interpreted as a reference to the GTP-bound Rap1, not a separate protein; for precise information, refer to standard naming Rap1 and Rap1GTP.