Disease relevance of STP-A11

• Several herpesvirus saimiri genes are potential candidates to cooperate with the gene for saimiri transformation-associated protein of subgroup A (STP-A) in T-lymphocyte growth stimulation [1].
• HVS-encoded proteins tyrosine-kinase interacting protein (Tip) and saimiri transformation-associated protein subgroup C (StpC) were previously implicated in altering HIV permissiveness [2].
• Herpesvirus saimiri (HVS)-transformed human T cells expressing terminal membrane proteins (TMPs) tyrosine kinase interacting protein (Tip) and saimiri transformation associated protein strain C (StpC) are highly permissive for R5 and X4 strains of HIV-1 [3].

High impact information on STP-A11

• The STP-A11 reading frame of strain 11 (subgroup A) was much less potent in its transforming ability than STP-C488 [4].
• One open reading frame, designated STP-C488 (for saimiri-transformation-associated protein of the subgroup C strain 488), phenotypically transformed Rat-1 cells, resulting in formation of foci, growth at reduced serum concentration, and growth to higher cell densities [4].
• Also, tyrosine phosphorylation of STP-A11 by src led to subsequent binding to lck and fyn in vitro [5].

Associations of STP-A11 with chemical compounds

• Mutational analysis of STP-A11 showed that binding to src kinase required the tyrosine residue at 115, showing that YAEV/I is a likely binding motif for src [5].

References