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At least 253 records · Page 14Linked to original sources
PubMed2005

Linking Rap to cell adhesion.

The small GTPase Rap1 is involved in several aspects of cell adhesion, including integrin-mediated cell adhesion and cadherin-mediated cell junction formation. Recently, several effector proteins for Rap1 have been identified providing a clear link between Rap1 and actin dynamics. Furthermore, evidence is accumulating that Rap1 functions in the spatial and temporal control of cell polarity.

Actin Cytoskeleton↗
PubMed2006

Differential G-alpha interaction capacities of the GoLoco motifs in Rap GTPase activating proteins.

GoLoco motif proteins act as guanine nucleotide dissociation inhibitors (GDIs) for G-protein alpha subunits of the adenylyl cyclase-inhibitory (Galpha(i/o)) class. Rap1GAP2 is a newly identified GoLoco motif- and RapGAP domain-containing protein, and thus is considered a potential integrator of heterotrimeric and monomeric GTPase signaling. Primary sequence analysis indicated that the Rap1GAP2 GoLoco motif contains a lysine (Lys-75), rather than an arginine, at the crucial residue responsible for binding the alpha and beta phosphates of GDP and exerting GDI activity. To determine the functional outcome of this sequence variation we conducted a biophysical analysis of the human Rap1GAP2b/c GoLoco motif. We found that human Rap1GAP2b/c was deficient in GDI activity and Galpha interaction capability. Mutation of lysine-75 to arginine could not regain functional activity of the Rap1GAP2b/c GoLoco motif. Thus, the Rap1GAP2b/c GoLoco motif can be classed as inactive towards Galpha subunits. We also found that the Rap1GAP1a GoLoco motif, which lacks seven N-terminal amino acid residues present in canonical GoLoco motifs, does not interact with Galpha(i1). In contrast, the GoLoco motif of Rap1GAP1b, which is canonical in primary sequence, was found to interact with Galpha(i1).GDP.

Amino Acid Motifs↗
PubMed2005

Ras and Rap: are former enemies now friends?

The small GTPase Rap1 was originally thought to function as an antagonist of Ras. A recent paper by provides evidence that Ras and Rap1 function in parallel to activate Raf downstream of the Torso receptor tyrosine kinase in Drosophila.

Animals↗
PubMed2004

RAP--a putative RNA-binding domain.

A novel approximately 60-residue domain has been identified in Homo sapiens MGC5297 and various other proteins in eukaryotes. Sequence searches reveal that the domain is particularly abundant in apicomplexans and is predicted to be involved in diverse RNA-binding activities.

Amino Acid Motifs↗