Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns

TY - JOUR

T1 - Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns

AU - Lundby, Alicia

AU - Hansen, Kasper Lage

AU - Weinert, Brian Tate

AU - Breinholt Bekker-Jensen, Dorte

AU - Secher, Anna

AU - Skovgaard, Tine

AU - Kelstrup, Christian

AU - Dmytriyev, Anatoliy

AU - Choudhary, Chuna Ram

AU - Lundby, Carsten

AU - Olsen, Jesper Velgaard

N1 - Copyright © 2012 The Authors. Published by Elsevier Inc. All rights reserved.

PY - 2012/8/30

Y1 - 2012/8/30

N2 - The local interaction of F-actin with myosin-II motor filaments and crosslinking proteins is crucial for the force generation, dynamics, and reorganization of the intracellular cytoskeleton. By using a bottom-up approach, we are able to show that the contractility of reconstituted active actin systems is tightly controlled by the local pH. The pH-dependent intrinsic crossbridge strength of myosin-II is identified to account for a sharp transition of the actin/myosin-II activity from noncontractile to contractile by a change in pH of only 0.1. This pH-dependent contractility is a generic feature, which is observed in all studied crosslinked actin/myosin-II systems. The specific type and concentration of crosslinking protein allows one to sensitively adjust the range of pH where contraction occurs, which can recover the behavior found in Xenopus laevis oocyte extracts. Small variations in pH provide a mechanism of controlling the contractility of cytoskeletal structures, which can be expected to have broad implications in our understanding of cytoskeletal regulation

AB - The local interaction of F-actin with myosin-II motor filaments and crosslinking proteins is crucial for the force generation, dynamics, and reorganization of the intracellular cytoskeleton. By using a bottom-up approach, we are able to show that the contractility of reconstituted active actin systems is tightly controlled by the local pH. The pH-dependent intrinsic crossbridge strength of myosin-II is identified to account for a sharp transition of the actin/myosin-II activity from noncontractile to contractile by a change in pH of only 0.1. This pH-dependent contractility is a generic feature, which is observed in all studied crosslinked actin/myosin-II systems. The specific type and concentration of crosslinking protein allows one to sensitively adjust the range of pH where contraction occurs, which can recover the behavior found in Xenopus laevis oocyte extracts. Small variations in pH provide a mechanism of controlling the contractility of cytoskeletal structures, which can be expected to have broad implications in our understanding of cytoskeletal regulation

KW - Faculty of Health and Medical Sciences

U2 - 10.1016/j.celrep.2012.07.006

DO - 10.1016/j.celrep.2012.07.006

M3 - Journal article

C2 - 22902405

SN - 2211-1247

VL - 2

SP - 419

EP - 431

JO - Cell Reports

JF - Cell Reports

IS - 2

ER -