A Third Musketeer on the ER: MOSPD2 is a Novel VAP-related Receptor for FFAT Motifs

Interorganelle membrane contact sites are subcellular structures that favor exchange and communication inside the cell. Such microdomains are built by molecular bridges that create a physical connection between two distinct organelles. The field of contact sites is now flourishing with discoveries o...

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Bibliographic Details
Published inContact Vol. 1
Main Authors Di Mattia, Thomas, Tomasetto, Catherine, Alpy, Fabien
Format Journal Article
LanguageEnglish
Published Los Angeles, CA SAGE Publications 01.01.2018
Sage Publications Ltd
Sage
SAGE Publishing
Subjects
Cell interactions
Cellular Biology
Endoplasmic reticulum
Endosomes
Golgi apparatus
Life Sciences
Mitochondria
Organelles
Proteins
Subcellular Processes
Tethering
membrane contact site
FFAT motif
endoplasmic reticulum (ER)
ER-organelle contact
VAP proteins
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Summary:Interorganelle membrane contact sites are subcellular structures that favor exchange and communication inside the cell. Such microdomains are built by molecular bridges that create a physical connection between two distinct organelles. The field of contact sites is now flourishing with discoveries of new tethering molecules. In that context, we identified by an unbiased proteomic approach a novel scaffold protein named MOtile SPerm Domain-containing protein 2 (MOSPD2). MOSPD2 is an endoplasmic reticulum (ER)-resident protein that is able to interact with several organelle-bound proteins that possess a small motif, named FFAT (two phenylalanines in an acidic tract). Consequently, we showed that MOSPD2 and its protein partners build contacts between the ER and endosomes, mitochondria, or Golgi. These findings highlight a new way for docking organelles on the ER.
ISSN:2515-2564
2515-2564
DOI:10.1177/2515256418809730