Unconventional secretion of transmembrane proteins

Heon Yung Gee, Jiyoon Kim, Min Goo Lee

Research output: Contribution to journalReview article

3 Citations (Scopus)

Abstract

Over the past 20 years it has become evident that eukaryotic cells utilize both conventional and unconventional pathways to deliver proteins to their target sites. Most proteins with a signal peptide and/or a transmembrane domain are conventionally transported through the endoplasmic reticulum to the Golgi apparatus and then to the plasma membrane. However, an increasing number of both soluble cargos (Type I, II, and III) and integral membrane proteins (Type IV) have been found to reach the plasma membrane via unconventional protein secretion (UPS) pathways that bypass the Golgi apparatus under certain conditions, such as cellular stress or development. Well-known examples of transmembrane proteins that undergo Type IV UPS pathways are position-specific antigen subunit alpha 1 integrin, cystic fibrosis transmembrane conductance regulator, myeloproliferative leukemia virus oncogene, and pendrin. Although we collectively refer to all Golgi-bypassing routes as UPS, individual trafficking pathways are diverse compared to the conventional pathways, and the molecular mechanisms of UPS pathways are not yet completely defined. This review summarizes the intracellular trafficking pathways of UPS cargo proteins, particularly those with transmembrane domains, and discusses the molecular machinery involved in the UPS of transmembrane proteins.

Original languageEnglish
Pages (from-to)59-66
Number of pages8
JournalSeminars in Cell and Developmental Biology
Volume83
DOIs
Publication statusPublished - 2018 Nov 1

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Proteins
Secretory Pathway
Golgi Apparatus
Integrin alpha1
Cell Membrane
Cystic Fibrosis Transmembrane Conductance Regulator
Eukaryotic Cells
Protein Sorting Signals
Oncogenes
Endoplasmic Reticulum
Membrane Proteins
Leukemia
Viruses
Antigens

All Science Journal Classification (ASJC) codes

  • Developmental Biology
  • Cell Biology

Cite this

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Unconventional secretion of transmembrane proteins. / Gee, Heon Yung; Kim, Jiyoon; Lee, Min Goo.

In: Seminars in Cell and Developmental Biology, Vol. 83, 01.11.2018, p. 59-66.

Research output: Contribution to journalReview article

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AU - Lee, Min Goo

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AB - Over the past 20 years it has become evident that eukaryotic cells utilize both conventional and unconventional pathways to deliver proteins to their target sites. Most proteins with a signal peptide and/or a transmembrane domain are conventionally transported through the endoplasmic reticulum to the Golgi apparatus and then to the plasma membrane. However, an increasing number of both soluble cargos (Type I, II, and III) and integral membrane proteins (Type IV) have been found to reach the plasma membrane via unconventional protein secretion (UPS) pathways that bypass the Golgi apparatus under certain conditions, such as cellular stress or development. Well-known examples of transmembrane proteins that undergo Type IV UPS pathways are position-specific antigen subunit alpha 1 integrin, cystic fibrosis transmembrane conductance regulator, myeloproliferative leukemia virus oncogene, and pendrin. Although we collectively refer to all Golgi-bypassing routes as UPS, individual trafficking pathways are diverse compared to the conventional pathways, and the molecular mechanisms of UPS pathways are not yet completely defined. This review summarizes the intracellular trafficking pathways of UPS cargo proteins, particularly those with transmembrane domains, and discusses the molecular machinery involved in the UPS of transmembrane proteins.

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