Phospholipid transfer function of PTPIP51 at mitochondria-associated ER membranes

Cited 43 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorH K Yeo-
dc.contributor.authorTA H Park-
dc.contributor.authorH Y Kim-
dc.contributor.authorH Jang-
dc.contributor.authorJ Lee-
dc.contributor.authorG S Hwang-
dc.contributor.authorS E Ryu-
dc.contributor.authorS H Park-
dc.contributor.authorH K Song-
dc.contributor.authorHyun Seung Ban-
dc.contributor.authorH J Yoon-
dc.contributor.authorB I Lee-
dc.date.accessioned2021-06-18T03:33:01Z-
dc.date.available2021-06-18T03:33:01Z-
dc.date.issued2021-
dc.identifier.issn1469-221X-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/24406-
dc.description.abstractIn eukaryotic cells, mitochondria are closely tethered to the endoplasmic reticulum (ER) at sites called mitochondria-associated ER membranes (MAMs). Ca2+ ion and phospholipid transfer occurs at MAMs to support diverse cellular functions. Unlike those in yeast, the protein complexes involved in phospholipid transfer at MAMs in humans have not been identified. Here, we determine the crystal structure of the tetratricopeptide repeat domain of PTPIP51 (PTPIP51_TPR), a mitochondrial protein that interacts with the ER-anchored VAPB protein at MAMs. The structure of PTPIP51_TPR shows an archetypal TPR fold, and an electron density map corresponding to an unidentified lipid-like molecule probably derived from the protein expression host is found in the structure. We reveal functions of PTPIP51 in phospholipid binding/transfer, particularly of phosphatidic acid, in vitro. Depletion of PTPIP51 in cells reduces the mitochondrial cardiolipin level. Additionally, we confirm that the PTPIP51-VAPB interaction is mediated by the FFAT-like motif of PTPIP51 and the MSP domain of VAPB. Our findings suggest that PTPIP51 is a phospholipid transfer protein with a MAM-tethering function.-
dc.publisherWiley-
dc.titlePhospholipid transfer function of PTPIP51 at mitochondria-associated ER membranes-
dc.title.alternativePhospholipid transfer function of PTPIP51 at mitochondria-associated ER membranes-
dc.typeArticle-
dc.citation.titleEMBO Reports-
dc.citation.number6-
dc.citation.endPagee51323-
dc.citation.startPagee51323-
dc.citation.volume22-
dc.contributor.affiliatedAuthorHyun Seung Ban-
dc.contributor.alternativeName예현구-
dc.contributor.alternativeName박태현-
dc.contributor.alternativeName김희연-
dc.contributor.alternativeName장현철-
dc.contributor.alternativeName이주은-
dc.contributor.alternativeName황금숙-
dc.contributor.alternativeName류성언-
dc.contributor.alternativeName박시훈-
dc.contributor.alternativeName송현규-
dc.contributor.alternativeName반현승-
dc.contributor.alternativeName윤혜진-
dc.contributor.alternativeName이병일-
dc.identifier.bibliographicCitationEMBO Reports, vol. 22, no. 6, pp. e51323-e51323-
dc.identifier.doi10.15252/embr.202051323-
dc.subject.keywordEndoplasmic reticulum-
dc.subject.keywordMAM-
dc.subject.keywordMitochondria-
dc.subject.keywordPhospholipid-
dc.subject.keywordPTPIP51-
dc.subject.localEndoplasmic reticulum (ER)-
dc.subject.localendoplasmic reticulum (ER)-
dc.subject.localEndoplasmic reticulum-
dc.subject.localendoplasmic reticulum-
dc.subject.localMAM-
dc.subject.localMitochondria-
dc.subject.localmitochondria-
dc.subject.localPhospholipid-
dc.subject.localPhospholipids-
dc.subject.localphospholipid-
dc.subject.localPTPIP51-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Biotherapeutics Translational Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.