scholarly journals Cellular Targets of the SV40 Small-t Antigen in Human Cell Transformation

Cell Cycle ◽  
2004 ◽  
Vol 3 (5) ◽  
pp. 604-608 ◽  
Author(s):  
Christine Skoczylas ◽  
Kelly M. Fahrbach ◽  
Kathleen Rundell
Virology ◽  
2001 ◽  
Vol 290 (2) ◽  
pp. 192-198 ◽  
Author(s):  
Jing Yu ◽  
Anita Boyapati ◽  
Kathleen Rundell

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Jong Wook Kim ◽  
Christian Berrios ◽  
Miju Kim ◽  
Amy E Schade ◽  
Guillaume Adelmant ◽  
...  

Alterations involving serine-threonine phosphatase PP2A subunits occur in a range of human cancers, and partial loss of PP2A function contributes to cell transformation. Displacement of regulatory B subunits by the SV40 Small T antigen (ST) or mutation/deletion of PP2A subunits alters the abundance and types of PP2A complexes in cells, leading to transformation. Here, we show that ST not only displaces common PP2A B subunits but also promotes A-C subunit interactions with alternative B subunits (B’’’, striatins) that are components of the Striatin-interacting phosphatase and kinase (STRIPAK) complex. We found that STRN4, a member of STRIPAK, is associated with ST and is required for ST-PP2A-induced cell transformation. ST recruitment of STRIPAK facilitates PP2A-mediated dephosphorylation of MAP4K4 and induces cell transformation through the activation of the Hippo pathway effector YAP1. These observations identify an unanticipated role of MAP4K4 in transformation and show that the STRIPAK complex regulates PP2A specificity and activity.


2008 ◽  
Vol 27 (2) ◽  
pp. 137-146 ◽  
Author(s):  
Anna A. Sablina ◽  
William C. Hahn

2019 ◽  
Author(s):  
Jong Wook Kim ◽  
Christian Berrios ◽  
Miju Kim ◽  
Amy E. Schade ◽  
Guillaume Adelmant ◽  
...  

AbstractAlterations involving serine-threonine phosphatase PP2A subunits occur in a range of human cancers and partial loss of PP2A function contributes to cell transformation. Displacement of regulatory B subunits by the SV40 Small T antigen (ST) or mutation/deletion of PP2A subunits alters the abundance and types of PP2A complexes in cells, leading to transformation. Here we show that ST not only displaces common PP2A B subunits but also promotes A-C subunit interactions with alternative B subunits (B’’’, striatins) that are components of the Striatin-interacting phosphatase and kinase (STRIPAK) complex. We found that STRN4, a member of STRIPAK, is associated with ST and is required for ST-PP2A-induced cell transformation. ST recruitment of STRIPAK facilitates PP2A-mediated dephosphorylation of MAP4K4 and induces cell transformation through the activation of the Hippo pathway effector YAP1. These observations identify an unanticipated role of MAP4K4 in transformation and show that the STRIPAK complex regulates PP2A specificity and activity.


Cell ◽  
1987 ◽  
Vol 48 (2) ◽  
pp. 321-330 ◽  
Author(s):  
Ilan Bikel ◽  
Ximena Montano ◽  
Mounzer E. Agha ◽  
Myles Brown ◽  
Melissa McCormack ◽  
...  

Oncogene ◽  
2019 ◽  
Vol 39 (10) ◽  
pp. 2170-2186 ◽  
Author(s):  
Kiyotaka Oshikawa ◽  
Masaki Matsumoto ◽  
Manabu Kodama ◽  
Hideyuki Shimizu ◽  
Keiichi I. Nakayama

1999 ◽  
Vol 251 (1) ◽  
pp. 121-127 ◽  
Author(s):  
Brian Whalen ◽  
Judith Laffin ◽  
Thomas D. Friedrich ◽  
John M. Lehman

2001 ◽  
Vol 284 (2) ◽  
pp. 369-376 ◽  
Author(s):  
Raphaëlle Gillet ◽  
Catherine Cavard ◽  
Gisèle Grimber ◽  
Pascale Briand ◽  
Virginie Joulin

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