4.6 Article

Pinning down viral proteins: a new prototype for virus-host cell interaction

Journal

FRONTIERS IN MICROBIOLOGY
Volume 1, Issue -, Pages -

Publisher

FRONTIERS RESEARCH FOUNDATION
DOI: 10.3389/fmicb.2010.00107

Keywords

phosphorylation; prolyl-isomerization; protein stability; Pin1

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Funding

  1. Takeda Science Foundation
  2. Japanese Ministry of Education
  3. Japanese Ministry of Culture
  4. Japanese Ministry of Sports
  5. Japanese Ministry of Science
  6. Japanese Ministry of Technology

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Pin1 is an enzyme that specifically catalyzes the cis-trans isomerization of phosphorylated serine/threonine-proline (pSer/Thr-Pro) motif in its substrate proteins. Recent studies demonstrate that stability of several viral proteins is regulated by phosphorylation-dependent prolyl-isomerization by a host factor Pin1. Pin1 is now positioned as an important modulator of the molecular crosstalk between virus and host cells and could be a unique target for anti-virus therapy. This new type of post-translational modification by Pin1 might be involved in the regulation of other viral proteins.

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