Paxillin isoforms in mouse: Lack of the γ isoform and developmentally specific β isoform expression

Yuichi Mazaki, Hiroshi Uchida, Okio Hino, Shigeru Hashimoto, Hisataka Sabe

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

Paxillin, a focal adhesion protein, exists as multiple isoforms in humans (α, β, and γ). To understand more about the physiological role of each isoform, we have employed the mouse system. We found that although the α and β isoforms are present in the mouse, the γ isoform is not. The α isoform protein was detected clearly in most adult tissues, whereas the β isoform protein was almost undetectable except in spleen, testis, thymus, and lung. On the other hand, mRNAs of both isoforms were detectable in all tissues we examined. High levels of the β isoform protein was detected in peritoneal exudate macrophage cells in adult mouse as well as in cultured fibroblasts, together with the α isoform. The α isoform was expressed at a constant level throughout the embryonic stages we examined, whereas the β isoform protein was detected at the mid-stages of development and increased to levels almost equal to those of the α isoform during the late stages of embryogenesis. Therefore, unlike the α isoform, expression of the β isoform protein is restricted in adult tissues. Moreover, we showed that α and β isoforms were colocalized within the same focal adhesion plaques, and cytoplasmic pools of both isoforms exist in the perinuclear area, colocalized with the Golgi apparatus.

Original languageEnglish
Pages (from-to)22435-22441
Number of pages7
JournalJournal of Biological Chemistry
Volume273
Issue number35
DOIs
Publication statusPublished - 1998 Aug 28

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Paxillin isoforms in mouse: Lack of the γ isoform and developmentally specific β isoform expression'. Together they form a unique fingerprint.

  • Cite this