Pinning down viral proteins: A new prototype for virus-host cell interaction
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...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2010-09-01
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| Series: | Frontiers in Microbiology |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fmicb.2010.00107/full |
| _version_ | 1819231673746718720 |
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| author | Yoshitsugu eKojima Akihide Ryo |
| author_facet | Yoshitsugu eKojima Akihide Ryo |
| author_sort | Yoshitsugu eKojima |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-23T11:48:42Z |
| format | Article |
| id | doaj.art-c1fdc9bf24784d2c9a73cfe6454d3aa3 |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-12-23T11:48:42Z |
| publishDate | 2010-09-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Microbiology |
| spelling | doaj.art-c1fdc9bf24784d2c9a73cfe6454d3aa32022-12-21T17:48:16ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2010-09-01110.3389/fmicb.2010.001072294Pinning down viral proteins: A new prototype for virus-host cell interactionYoshitsugu eKojima0Akihide Ryo1Yokohama City University School of MedicineYokohama City University School of MedicinePin1 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.http://journal.frontiersin.org/Journal/10.3389/fmicb.2010.00107/fullPhosphorylationProtein StabilityPin1Prolyl-isomerazation |
| spellingShingle | Yoshitsugu eKojima Akihide Ryo Pinning down viral proteins: A new prototype for virus-host cell interaction Frontiers in Microbiology Phosphorylation Protein Stability Pin1 Prolyl-isomerazation |
| title | Pinning down viral proteins: A new prototype for virus-host cell interaction |
| title_full | Pinning down viral proteins: A new prototype for virus-host cell interaction |
| title_fullStr | Pinning down viral proteins: A new prototype for virus-host cell interaction |
| title_full_unstemmed | Pinning down viral proteins: A new prototype for virus-host cell interaction |
| title_short | Pinning down viral proteins: A new prototype for virus-host cell interaction |
| title_sort | pinning down viral proteins a new prototype for virus host cell interaction |
| topic | Phosphorylation Protein Stability Pin1 Prolyl-isomerazation |
| url | http://journal.frontiersin.org/Journal/10.3389/fmicb.2010.00107/full |
| work_keys_str_mv | AT yoshitsuguekojima pinningdownviralproteinsanewprototypeforvirushostcellinteraction AT akihideryo pinningdownviralproteinsanewprototypeforvirushostcellinteraction |