Skip to main navigation Skip to search Skip to main content

Cloning of a SH3 domain-containing proline-rich protein, p85SPR, and its localization in focal adhesion

  • Woo Kyun Oh
  • , Jae Cheal Yoo
  • , Donggyu Jo
  • , Young Hwa Song
  • , Moon Gyo Kim
  • , Dongeun Park
  • Gwangju Institute of Science and Technology
  • National Institutes of Health

Research output: Contribution to journalArticlepeer-review

Abstract

A mouse thymus cDNA expression library was screened with monoclonal antibody (mAb), B16-5 which binds to common epitope in SH3 domains of phospholipase C-γ 1 (PLC-γ 1) and Nck. We have determined the complete nucleotide sequence of one of several positive clones. The 4,172 bp cDNA clone (Gen-Bank Accession No. U96634) encodes a SH3 domain-containing protein of 646 amino acids. Besides the SH3 domain, the predicted protein has a proline-rich region, nuclear localization signals, and leucine zipper motifs. The expressed protein in Sf9 insect cell exhibits a polypeptide of 85 kDa on SDS-PAGE. The protein is widely distributed in rat tissue with an especially high level of expression in brain and testis. Interestingly, the specific antibodies detected four related proteins of different size (75, 85, 90 and 105 kDa) in brain. In A431 cell, p85SPR is enriched at focal adhesion points indicating that the protein may interact with protein(s) in focal complexes.

Original languageEnglish
Pages (from-to)794-798
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume235
Issue number3
DOIs
StatePublished - 27 Jun 1997
Externally publishedYes

Fingerprint

Dive into the research topics of 'Cloning of a SH3 domain-containing proline-rich protein, p85SPR, and its localization in focal adhesion'. Together they form a unique fingerprint.

Cite this