Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Protein energetics in maturation of the early secretory pathway

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

related to degree

  • Wiseman, R. Luke, Ph.D. in Chemistry, Scripps Research 2001 - 2005

authors

  • Wiseman, R. Luke
  • Koulov, A.
  • Powers, Evan
  • Kelly, Jeffery
  • Balch, William E.

publication date

  • August 2007

journal

  • Current Opinion in Cell Biology  Journal

abstract

  • The early secretory pathway (ESP) consisting of the endoplasmic reticulum (ER), pre-Golgi intermediates and the Golgi stack links protein synthesis to folding and vesicle trafficking to generate the membrane architecture of the eukaryotic cell. The fundamental principles that contribute to organization of the ESP remain largely unknown. We raise the possibility that assembly of the ESP is largely built on a foundation that is influenced by the kinetic and thermodynamic properties of the protein fold. Folding energetics may provide an adjustable platform for adaptor-dependent interactions with the transport machinery, suggesting the possibility that protein cargo energetics plays a central role in directing both trafficking patterns and global compartmental organization of the ESP. In this view, cargo energetics likely coordinates the composition and maturation of ER and Golgi compartments with the physiological state of the cell in different tissue and environmental settings.

subject areas

  • Animals
  • Energy Metabolism
  • Humans
  • Protein Folding
  • Proteins
  • Secretory Vesicles
  • Signal Transduction
scroll to property group menus

Identity

PubMed Central ID

  • PMC2094714

International Standard Serial Number (ISSN)

  • 0955-0674

Digital Object Identifier (DOI)

  • 10.1016/j.ceb.2007.05.005

PubMed ID

  • 17686625
scroll to property group menus

Additional Document Info

start page

  • 359

end page

  • 367

volume

  • 19

issue

  • 4

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support