Neuronal protein NP25 interacts with F-actin

• Published in: Neuroscience research Vol. 48; no. 4; pp. 439 - 446
• Main Authors: Mori, Kenji, Muto, Yoshinori, Kokuzawa, Jouji, Yoshioka, Takashi, Yoshimura, Shinichi, Iwama, Toru, Okano, Yukio, Sakai, Noboru
• Format: Journal Article
• Language: English
• Published: Ireland Elsevier Ireland Ltd 01.04.2004
• Subjects: Actin-binding protein; Actins - metabolism; Animals; Blotting, Western; Cell Line, Tumor; Cytoskeleton - metabolism; F-actin; FRET; Immunohistochemistry; Microscopy, Fluorescence; Nerve Tissue Proteins - metabolism; Neuroblastoma - metabolism; Neuronal protein 25; SK-N-SH; PBS; NP25; CH domain; TBST; GST; SDS–PAGE; Actin-binding protein; BSA; Neuronal protein 25; F-actin; PMSF; CLRs; FBS; SK-N-SH; FRET
• ISSN: 0168-0102; 1872-8111
• DOI: 10.1016/j.neures.2003.12.012

Neuronal protein NP25 is a neuron-specific protein present in highly differentiated neural cells, but its functional properties have not been well characterized. NP25 shows high amino acid sequence homology with the smooth muscle cell cytoskeleton-associated proteins, SM22, mp20, and calponin. To gain an insight into the biological functions of NP25, we first examined its subcellular localization in the human neuroblastoma cell line, SK-N-SH. NP25 diffusely distributed in the cytoplasm and fiber-like staining was also observed. It showed that NP25 co-localized with F-actin on stress fibers. A co-sedimentation assay demonstrated that NP25 bound to filamentous actin. Further investigations using fluorescence resonance energy transfer (FRET) technique revealed intracellular binding of NP25 and actin. The significance of the interaction between NP25 and F-actin is discussed.