Molecular mechanisms of aquaporin biogenesis by the endoplasmic reticulum Sec61 translocon

David Pitonzo, William Skach

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

The past decade has witnessed remarkable advances in our understanding of aquaporin (AQP) structure and function. Much, however, remains to be learned regarding how these unique and vitally important molecules are generated in living cells. A major obstacle in this respect is that AQP biogenesis takes place in a highly specialized and relatively inaccessible environment formed by the ribosome, the Sec61 translocon and the ER membrane. This review will contrast the folding pathways of two AQP family members, AQP1 and AQP4, and attempt to explain how six TM helices can be oriented across and integrated into the ER membrane in the context of current (and somewhat conflicting) translocon models. These studies indicate that AQP biogenesis is intimately linked to translocon function and that the ribosome and translocon form a highly dynamic molecular machine that both interprets and is controlled by specific information encoded within the nascent AQP polypeptide. AQP biogenesis thus has wide ranging implications for mechanisms of translocon function and general membrane protein folding pathways.

Original languageEnglish (US)
Pages (from-to)976-988
Number of pages13
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1758
Issue number8
DOIs
StatePublished - Aug 2006

Fingerprint

Aquaporins
Endoplasmic Reticulum
Ribosomes
Membranes
Protein folding
Protein Folding
Molecular Dynamics Simulation
Molecular dynamics
Membrane Proteins
Cells
Peptides
Molecules

Keywords

  • Aquaporin
  • Biogenesis
  • Endoplasmic reticulum
  • ER
  • Polytopic protein
  • Sec61
  • Translocon

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Biophysics

Cite this

Molecular mechanisms of aquaporin biogenesis by the endoplasmic reticulum Sec61 translocon. / Pitonzo, David; Skach, William.

In: Biochimica et Biophysica Acta - Biomembranes, Vol. 1758, No. 8, 08.2006, p. 976-988.

Research output: Contribution to journalArticle

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