Identification of a novel human lysophosphatidic acid acyltransferase, LPAAT-theta, which activates mTOR pathway

Wenwen Tang, Jian Yuan, Xinya Chen, Xiuting Gu, Kuntian Luo, Jie Li, Bo Wan, Yingli Wang, Long Yu

Research output: Contribution to journalArticlepeer-review

42 Scopus citations

Abstract

Lysophosphatidic acid acyltransferase (LPAAT) is an intrinsic membrane protein that catalyzes the synthesis of phosphatidic acid (PA) from lysophosphatidic acid (LPA). It is well known that LPAAT is involved in lipid biosynthesis, while its role in tumour progression has been of emerging interest in the last few years. To date, seven members of the LPAAT gene family have been found in human. Here we report a novel LPAAT member, designated as LPAAT-theta, which was 2728 base pairs in length and contained an open reading frame (ORF) encoding 434 amino acids. The LPAAT-theta gene consisted of 12 exons and 11 introns, and mapped to chromosome 4q21.23. LPAAT-theta was ubiquitously expressed in 18 human tissues by RT-PCR analysis. Subcellular localization of LPAAT-theta-EGFP fusion protein revealed that LPAAT-theta was distributed primarily in the endoplasmic reticulum (ER) of COS-7 cells. Furthermore, we found that the overexpression of LPAAT-theta can induce mTOR-dependent p70S6K phosphorylation on Thr389 and 4EBP1 phosphorylation on Ser65 in HEK293T cells.

Original languageEnglish (US)
Pages (from-to)626-635
Number of pages10
JournalJournal of Biochemistry and Molecular Biology
Volume39
Issue number5
DOIs
StatePublished - Sep 2006

Keywords

  • 4EBP1
  • Endoplasmic reticulum
  • Lysophosphatidic acid acyltransferase
  • mTOR
  • p70S6K

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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