(PDF) Multisite Phosphorylation of S6K1 Directs a Kinase

Multisite Phosphorylation of S6K1 Directs a Kinase Phospho-Code That Determines Substrate Selection

Molecular Cell - United States

doi 10.1016/j.molcel.2018.11.017

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February 1, 2019

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Multisite Phosphorylation of S6K1 Directs a Kinase Phospho-Code That Determines Substrate Selection

Molecular Cell - United States

doi 10.1016/j.molcel.2018.11.017

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

A Combination of Multisite Phosphorylation and Substrate Sequestration Produces Switchlike Responses

Applying the Brakes to Multisite SR Protein Phosphorylation: Substrate-Induced Effects on the Splicing Kinase SRPK1

Tyrosine-1 and Threonine-4 Phosphorylation Marks Complete the RNA Polymerase II CTD Phospho-Code

Regulation ofYersiniaProtein Kinase a (YpkA) Kinase Activity by Multisite Autophosphorylation and Identification of an N-Terminal Substrate-Binding Domain in YpkA

Phosphorylation of RAF Kinase Dimers Drives Conformational Changes That Facilitate Transactivation

Integrin-Linked Kinase Is a Functional Mn2+-Dependent Protein Kinase That Regulates Glycogen Synthase Kinase-3β (GSK-3β) Phosphorylation

Stimulus-Dependent Phosphorylation of MacMARCKS, a Protein Kinase C Substrate, in Nerve Termini and PC12 Cells

Identification of Mechanism That Couples Multisite Phosphorylation of Yes-Associated Protein (YAP) With Transcriptional Coactivation and Regulation of Apoptosis

Prolactin Activates Tyrosyl Phosphorylation of Insulin Receptor Substrate 1 and Phosphatidylinositol-3-Oh Kinase