Journal article

Dual requirement for a newly identified phosphorylation site in p70(s6k)

BA Moser, PB Dennis, N Pullen, RB Pearson, NA Williamson, REH Wettenhall, SC Kozma, G Thomas

Molecular and Cellular Biology | AMER SOC MICROBIOLOGY | Published : 1997

Abstract

The activation of p70s6k is associated with multiple phosphorylations at two sets of sites. The first set, S411, S418, T421, and S424, reside within the autoinhibitory domain, and each contains a hydrophobic residue at -2 and a proline at +1. The second set of sites, T229 (in the catalytic domain) and T389 and S404 (in the linker region), are rapamycin sensitive and flanked by bulky aromatic residues. Here we describe the identification and mutational analysis of three new phosphorylation sites, T367, S371, and T447, all of which have a recognition motif similar to that of the first set of sites. A mutation of T367 or T447 to either alanine or glutamic acid had no apparent effect on p70s6k a..

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