Regulation of N-cadherin-based cell-cell interaction by JSAP1 scaffold in PC12h cells

Munkhuu Bayarsaikhan, Takahisa Takino, Davaakhuu Gantulga, Hiroshi Sato, Takashi Ito, Katsuji Yoshioka

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

We previously reported that the level of c-Jun NH2-terminal kinase (JNK)/stress-activated protein kinase-associated protein 1 (JSAP1), a scaffold protein for JNK signaling, increases dramatically during nerve growth factor (NGF)-induced differentiation of PC12h cells. In the present study, we investigated the function of JSAP1 during PC12h cell differentiation by knocking down the level of JSAP1. The depletion of JSAP1 caused NGF-treated PC12h cells to form aggregates and impaired their differentiation. The aggregation was not observed in JSAP1-depleted cells that were untreated or treated with epidermal growth factor. Immunocytochemical studies indicated that N-cadherin, but not E-cadherin, was localized to sites of cell-cell contact in the aggregated cells. Furthermore, an inhibitory anti-N-cadherin antibody completely blocked the aggregation. Taken together, these results suggest that JSAP1 regulates cell-cell interactions in PC12h cells specifically in the NGF-induced signaling pathway, and does so by modulating N-cadherin.

Original languageEnglish
Pages (from-to)357-362
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume353
Issue number2
DOIs
Publication statusPublished - Feb 9 2007

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Regulation of N-cadherin-based cell-cell interaction by JSAP1 scaffold in PC12h cells'. Together they form a unique fingerprint.

Cite this