Protein N-Myristoylation Is Required for Cellular Morphological Changes Induced by Two Formin Family Proteins, FMNL2 and FMNL3

• MORIYA Koko

  Applied Molecular Bioscience, Graduate School of Medicine, Yamaguchi University

• YAMAMOTO Takuo

  Applied Molecular Bioscience, Graduate School of Medicine, Yamaguchi University

• TAKAMITSU Emi

  Applied Molecular Bioscience, Graduate School of Medicine, Yamaguchi University

• MATSUNAGA Yukari

  Applied Molecular Bioscience, Graduate School of Medicine, Yamaguchi University

• KIMOTO Mayumi

  Applied Molecular Bioscience, Graduate School of Medicine, Yamaguchi University

• FUKUSHIGE Daichi

  Applied Molecular Bioscience, Graduate School of Medicine, Yamaguchi University

• KIMOTO Chihiro

  Applied Molecular Bioscience, Graduate School of Medicine, Yamaguchi University

• SUZUKI Takashi

  Clinical and Biotechnology Business Unit, Shimadzu Corporation

• UTSUMI Toshihiko

  Applied Molecular Bioscience, Graduate School of Medicine, Yamaguchi University Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University

Bibliographic Information

Other Title

• Protein <italic>N</italic>-myristoylation is required for cellular morphological changes induced by two formin family proteins, FMNL2 and FMNL3

Abstract

The subcellular localization of 13 recently identified N-myristoylated proteins and the effects of overexpression of these proteins on cellular morphology were examined with the aim of understanding the physiological roles of the protein N-myristoylation that occurs on these proteins. Immunofluorescence staining of HEK293T cells transfected with cDNAs coding for the proteins revealed that most of them were associated with the plasma membrane or the membranes of intracellular compartments, and did not affect cellular morphology. However, two proteins, formin-like2 (FMNL2) and formin-like3 (FMNL3), both of them are members of the formin family of proteins, were associated mainly with the plasma membrane and induced significant cellular morphological changes. Inhibition of protein N-myristoylation by replacement of Gly2 with Ala or by the use of N-myristoylation inhibitor significantly inhibited membrane localization and the induction of cellular morphological changes, indicating that protein N-myristoylation plays critical roles in the cellular morphological changes induced by FMNL2 and FMNL3.

Journal

• Bioscience, Biotechnology, and Biochemistry

  Bioscience, Biotechnology, and Biochemistry 76 (6), 1201-1209, 2012

  Japan Society for Bioscience, Biotechnology, and Agrochemistry

Keywords

• protein N-myristoylation
• formin-like2 (FMNL2)
• formin-like3 (FMNL3)
• formin family protein
• cellular morphological change

Details

• CRID: 1390282681454742016
• NII Article ID: 10030818388
• NII Book ID: AA10824164
• DOI: 10.1271/bbb.120069
• COI: 1:STN:280:DC%2BC38jps1GgtA%3D%3D
• ISSN: 13476947
• ISSN: 09168451
• NDL BIB ID: 023768535
• PubMed: 22790947
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I023768535
• Text Lang: en
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • PubMed
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed