From antibodies to adiponectin: Role of ERp44 in sizing and timing protein secretion

M. Cortini, R. Sitia

Research output: Contribution to journalArticlepeer-review

Abstract

A large fraction of the proteome is synthesized and folded in the endoplasmic reticulum (ER), a multifunctional compartment also playing pivotal roles in Ca2+ storage, redox homeostasis and signalling. From the ER, secretory proteins begin their journey towards their final destinations, the organelles of the exocytic and endocytic compartments, the plasma membrane or the extracellular space. Fidelity of protein-based intracellular communication is guaranteed by quality control (QC) mechanisms located at the ER-Golgi interface, which restrict forward transport to native proteins. QC is used also to time or shape the secretome. Furthermore, professional secretory cells face a problem of quantity, as well as quality of their protein products. This essay summarizes recent findings that identify ERp44 as a key regulator of protein secretion, Ca2+ signalling and redox regulation.

Original languageEnglish
Pages (from-to)39-47
Number of pages9
JournalDiabetes, Obesity and Metabolism
Volume12
Issue numberSUPPL. 2
DOIs
Publication statusPublished - Oct 2010

Keywords

  • Early secretory pathway
  • Endoplasmic reticulum
  • ERAD
  • Protein quality control
  • Secretion

ASJC Scopus subject areas

  • Internal Medicine
  • Endocrinology
  • Endocrinology, Diabetes and Metabolism

Fingerprint Dive into the research topics of 'From antibodies to adiponectin: Role of ERp44 in sizing and timing protein secretion'. Together they form a unique fingerprint.

Cite this