Formation of Intracellular Concentration Landscapes by Multisite Protein Modification

Files in This Item:
File Description SizeFormat 
Paper22.pdf1.01 MBAdobe PDFDownload
Title: Formation of Intracellular Concentration Landscapes by Multisite Protein Modification
Authors: Muñoz-García, Javier
Kholodenko, Boris N.
Neufeld, Zoltán
Permanent link: http://hdl.handle.net/10197/5041
Date: Jul-2010
Abstract: Multiple cellular proteins are covalently modified (e.g., phosphorylated/dephosphorylated) at several sites, which leads to diverse signaling activities. Here, we consider a signaling cascade that is activated at the plasma membrane and composed of two-site protein modification cycles, and we focus on the radial profile of the concentration landscapes created by different protein forms in the cytoplasm. We show that under proper conditions, the concentrations of modified proteins generate a series of peaks that propagate into the cell interior. Proteins modified at both sites form activity gradients with long plateaus that abruptly decay at successive locations along the path from the membrane to the nucleus. We demonstrate under what conditions signals generated at the membrane stall in the vicinity of that membrane or propagate into the cell. We derive analytical approximations for the main characteristics of the protein concentration profiles and demonstrate what we believe to be a novel steady-state pattern formation mechanism capable of generating precise spatial guidance for diverse cellular processes.
Type of material: Journal Article
Publisher: Elsevier
Copyright (published version): 2010 Elsevier
Keywords: intracellular concentration landscapes;multisite protein modification;protein concentration profiles
DOI: 10.1016/j.bpj.2010.04.014
Language: en
Status of Item: Peer reviewed
Appears in Collections:SBI Research Collection

Show full item record

SCOPUSTM   
Citations 50

2
Last Week
0
Last month
checked on Jun 22, 2018

Page view(s) 50

31
checked on May 25, 2018

Download(s) 50

33
checked on May 25, 2018

Google ScholarTM

Check

Altmetric


This item is available under the Attribution-NonCommercial-NoDerivs 3.0 Ireland. No item may be reproduced for commercial purposes. For other possible restrictions on use please refer to the publisher's URL where this is made available, or to notes contained in the item itself. Other terms may apply.