A novel protein encoded by Kaposi's sarcoma-associated herpesvirus open reading frame 36 inhibits cell spreading and focal adhesion kinase activation

Junsoo Park, Myung Shin Lee, Seung Min Yoo, Taegun Seo

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Objective: Kaposi's sarcoma-associated herpesvirus (KSHV) is a γ-herpesvirus implicated in the development of Kaposi's sarcoma, primary effusion lymphoma and some forms of multicentric Castleman's disease. The KSHV open reading frame (ORF) 36 encodes a viral serine/threonine protein kinase. The aim of this study was to characterize the cellular function of the ORF36 protein. Methods: The expression kinetics of the ORF36 protein and its localization were determined. The wild-type ORF36 and its mutant proteins were subjected to in vitro kinase assay. Cell morphology change by ORF36 protein was studied. The focal adhesion kinase (FAK) tyrosine phosphorylation and cleavage were determined when ORF36 was expressed. Results: ORF36 protein expressed in the late phase during the KSHV reactivation. The C-terminal domain of ORF36 protein was important for kinase activity. Moreover, the ORF36 protein altered cell morphology to a round shape, similar to the phenotype of FAK-deficient cells. The kinase activity of ORF36 protein was required for the inhibition of cell spreading. Interestingly, ORF36 protein colocalized with FAK, suppressed its tyrosine phosphorylation and promoted FAK cleavage. Conclusion: Our results collectively demonstrate that the KSHV ORF36 protein is a viral protein kinase that inhibits cell spreading and FAK activation.

Original languageEnglish
Pages (from-to)426-432
Number of pages7
JournalIntervirology
Volume50
Issue number6
DOIs
Publication statusPublished - 2008 Feb 1

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Human Herpesvirus 8
Focal Adhesion Protein-Tyrosine Kinases
Cell Adhesion
Open Reading Frames
Proteins
Phosphotransferases
Tyrosine
Primary Effusion Lymphoma
Phosphorylation
Kaposi's Sarcoma
Herpesviridae
Protein-Serine-Threonine Kinases
Viral Proteins
Mutant Proteins
Protein Kinases
Phenotype

All Science Journal Classification (ASJC) codes

  • Virology
  • Infectious Diseases

Cite this

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title = "A novel protein encoded by Kaposi's sarcoma-associated herpesvirus open reading frame 36 inhibits cell spreading and focal adhesion kinase activation",
abstract = "Objective: Kaposi's sarcoma-associated herpesvirus (KSHV) is a γ-herpesvirus implicated in the development of Kaposi's sarcoma, primary effusion lymphoma and some forms of multicentric Castleman's disease. The KSHV open reading frame (ORF) 36 encodes a viral serine/threonine protein kinase. The aim of this study was to characterize the cellular function of the ORF36 protein. Methods: The expression kinetics of the ORF36 protein and its localization were determined. The wild-type ORF36 and its mutant proteins were subjected to in vitro kinase assay. Cell morphology change by ORF36 protein was studied. The focal adhesion kinase (FAK) tyrosine phosphorylation and cleavage were determined when ORF36 was expressed. Results: ORF36 protein expressed in the late phase during the KSHV reactivation. The C-terminal domain of ORF36 protein was important for kinase activity. Moreover, the ORF36 protein altered cell morphology to a round shape, similar to the phenotype of FAK-deficient cells. The kinase activity of ORF36 protein was required for the inhibition of cell spreading. Interestingly, ORF36 protein colocalized with FAK, suppressed its tyrosine phosphorylation and promoted FAK cleavage. Conclusion: Our results collectively demonstrate that the KSHV ORF36 protein is a viral protein kinase that inhibits cell spreading and FAK activation.",
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A novel protein encoded by Kaposi's sarcoma-associated herpesvirus open reading frame 36 inhibits cell spreading and focal adhesion kinase activation. / Park, Junsoo; Lee, Myung Shin; Yoo, Seung Min; Seo, Taegun.

In: Intervirology, Vol. 50, No. 6, 01.02.2008, p. 426-432.

Research output: Contribution to journalArticle

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AB - Objective: Kaposi's sarcoma-associated herpesvirus (KSHV) is a γ-herpesvirus implicated in the development of Kaposi's sarcoma, primary effusion lymphoma and some forms of multicentric Castleman's disease. The KSHV open reading frame (ORF) 36 encodes a viral serine/threonine protein kinase. The aim of this study was to characterize the cellular function of the ORF36 protein. Methods: The expression kinetics of the ORF36 protein and its localization were determined. The wild-type ORF36 and its mutant proteins were subjected to in vitro kinase assay. Cell morphology change by ORF36 protein was studied. The focal adhesion kinase (FAK) tyrosine phosphorylation and cleavage were determined when ORF36 was expressed. Results: ORF36 protein expressed in the late phase during the KSHV reactivation. The C-terminal domain of ORF36 protein was important for kinase activity. Moreover, the ORF36 protein altered cell morphology to a round shape, similar to the phenotype of FAK-deficient cells. The kinase activity of ORF36 protein was required for the inhibition of cell spreading. Interestingly, ORF36 protein colocalized with FAK, suppressed its tyrosine phosphorylation and promoted FAK cleavage. Conclusion: Our results collectively demonstrate that the KSHV ORF36 protein is a viral protein kinase that inhibits cell spreading and FAK activation.

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