Department of Biotechnology and Bioinformatics, University of Kashmir, Jammu and Kashmir, India
Research Article
Phosphorylation State of S6K1 is Redundant for its Blood Interaction with F Actin
Author(s): Shafat A Latoo* and Khurshid I Andrabi
The evolutionarily conserved kinase (S6K1) that is actuated in response to certain stimulants like insulin, amino acids
and several other growth factors has emerged as a major effector of growth and proliferation of blood cells. In certain
types of cancers, the S6K1 a serine/threonine kinase is constantly actuated and acts as a downstream effector of the
Akt/phosphatidylinositol 3-kinase pathway. S6K1 serves to cross-link actin filament and activates the Rho family of
Guanosine Triphosphate (GTPases). We here present the evidence for domain-specific interaction of S6 kinase 1
(S6K1) with filamentous actin or F actin. We showed for the first time that the [ΔNH2-146/ΔCT240 a. acid] region of
S6K1 is responsible for its discrete binding to F actin. We also demonstrate that S6K1 binding to filamentous actin is
phosphorylation independ.. View more»