Human VAPome Analysis Reveals MOSPD1 and MOSPD3 as Membrane Contact Site Proteins Interacting with FFAT-Related FFNT Motifs

(Cell Reports 33, 108475; December 8, 2020) When this article was originally published on December 8, 2020, the accession number associated with the MS raw data (PRIDE: PXD01547) did not grant readers access to those data on the PRIDE database. The MS raw data are now accessible through the PRIDE database at PRIDE: PXD043399. The authors sincerely apologize for any inconvenience or confusion that may have resulted from the initial lack of accessibility to these data. Human VAPome Analysis Reveals MOSPD1 and MOSPD3 as Membrane Contact Site Proteins Interacting with FFAT-Related FFNT MotifsCabukusta et al.Cell ReportsDecember 08, 2020In BriefCabukusta et al. characterize MOSPD1 and MOSPD3 as members of the ER-resident VAP protein family interacting with short linear motif. Unlike VAPA, VAPB, and MOSPD2, MOSPD1 and MOSPD3 do not interact with canonical FFAT motifs but prefer unconventional motifs related to FFAT or FFNT motifs. Full-Text PDF Open Access