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PMID: 17942604 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Endocytic trafficking of sphingomyelin depends on its acyl chain length.

Molecular biology of the cell ·Vol. 18 ·No. 12 ·2007-12-00 ·Pages 5113-23

Koivusalo M, Jansen M, Somerharju P, Ikonen E

Abstract

To study the principles of endocytic lipid trafficking, we introduced pyrene sphingomyelins (PyrSMs) with varying acyl chain lengths and domain partitioning properties into human fibroblasts or HeLa cells. We found that a long-chain, ordered-domain preferring PyrSM was targeted Hrs and Tsg101 dependently to late endosomal compartments and recycled to the plasma membrane in an NPC1- and cholesterol-dependent manner. A short-chain, disordered domain preferring PyrSM recycled more effectively, by using Hrs-, Tsg101- and NPC1-independent routing that was insensitive to cholesterol loading. Similar chain length-dependent recycling was observed for unlabeled sphingomyelins (SMs). The findings 1) establish acyl chain length as an important determinant in the endocytic trafficking of SMs, 2) implicate ESCRT complex proteins and NPC1 in the endocytic recycling of ordered domain lipids to the plasma membrane, and 3) introduce long-chain PyrSM as the first fluorescent lipid tracing this pathway.

MeSH Terms
Biological Transport Cell Line Cell Membrane/metabolism Endocytosis Fibroblasts Humans Lysosomes/metabolism Molecular Structure Pyrenes/chemistry,metabolism Sphingomyelins/chemistry,metabolism
Chemicals
Pyrenes Sphingomyelins pyrene
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Koivusalo Mirkka
Institute of Biomedicine/Anatomy and Institute of Biomedicine/Biochemistry, University of Helsinki, FIN-00014, Helsinki, Finland.
Jansen Maurice
Somerharju Pentti
Ikonen Elina
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Article Info
Journal
Molecular biology of the cell
Abbr.
Mol Biol Cell
ISSN
1059-1524
Published
2007-12-00
Epub
2007-00-17
Pages
5113-23
Language
English
Region
United States
NLM ID
9201390
PMCID
PMC2096594
Subset
IM
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