A novel phospholipase A1 with sequence homology to a mammalian Sec23p-interacting protein, p125

Ken Ichi Nakajima, Hirofumi Sonoda, Toshihide Mizoguchi, Junken Aoki, Hiroyuki Arai, Masami Nagahama, Mitsuo Tagaya, Katsuko Tani

Research output: Contribution to journalArticle

72 Citations (Scopus)

Abstract

p125, a mammalian Sec23p-interacting protein, exhibits sequence homology with bovine testis phosphatidic acid-preferring phospholipase A1. In this study, we identified and characterized a new homologue of p125, KIAA0725p. KIAA0725p exhibited remarkable sequence similarity with p125 throughout the entire sequence determined but lacked an N-terminal proline-rich, Sec23p-interacting region. In vitro binding analysis showed that KIAA0725p does not bind to Sec23p. KIAA0725p possessed phospholipase A1 activity preferentially for phosphatidic acid. We examined the effects of overexpression of KIAA0725p on the morphology of organelles. Overexpression of KIAA0725p, like that of p125, caused dispersion of the endoplasmic reticulum-Golgi intermediate compartment and Golgi apparatus. Different from the case of p125, overexpression of KIAA0725p resulted in dispersion of tethering proteins located in the Golgi region and caused aggregation of the endoplasmic reticulum. Our results indicate that KIAA0725p is a new member of the phosphatidic acid-preferring phospholipase A1 protein family and suggest that the cellular function of KIAA0725p is different from that of p125.

Original languageEnglish
Pages (from-to)11329-11335
Number of pages7
JournalJournal of Biological Chemistry
Volume277
Issue number13
DOIs
Publication statusPublished - 2002 Mar 29
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'A novel phospholipase A<sub>1</sub> with sequence homology to a mammalian Sec23p-interacting protein, p125'. Together they form a unique fingerprint.

Cite this