Auxin transportGarbers, C., DeLong, A., Deruére, J., Bernasconi, P. and Söll, D. (1996) A mutation in protein phosphatase 2A regulatory subunit A affects auxin transport in Arabidopsis, EMBO J. 15, 2115–2124

1996 ◽  
Vol 1 (7) ◽  
pp. 211-211
1996 ◽  
Vol 15 (9) ◽  
pp. 2115-2124 ◽  
Author(s):  
C. Garbers ◽  
A. DeLong ◽  
J. Deruére ◽  
P. Bernasconi ◽  
D. Söll

2000 ◽  
Vol 64 (2) ◽  
pp. 438-442 ◽  
Author(s):  
Takayuki ISHIZAKI ◽  
Hiroshi YOKOYAMA ◽  
Susumu KAJIWARA ◽  
Kazuo SHISHIDO

2011 ◽  
Vol 156 (3) ◽  
pp. 1464-1480 ◽  
Author(s):  
Andrea Trotta ◽  
Michael Wrzaczek ◽  
Judith Scharte ◽  
Mikko Tikkanen ◽  
Grzegorz Konert ◽  
...  

2006 ◽  
Vol 26 (7) ◽  
pp. 2832-2844 ◽  
Author(s):  
Hugh K. Arnold ◽  
Rosalie C. Sears

ABSTRACT Protein phosphatase 2A (PP2A) plays a prominent role in controlling accumulation of the proto-oncoprotein c-Myc. PP2A mediates its effects on c-Myc by dephosphorylating a conserved residue that normally stabilizes c-Myc, and in this way, PP2A enhances c-Myc ubiquitin-mediated degradation. Stringent regulation of c-Myc levels is essential for normal cell function, as c-Myc overexpression can lead to cell transformation. Conversely, PP2A has tumor suppressor activity. Uncovering relevant PP2A holoenzymes for a particular target has been limited by the fact that cellular PP2A represents a large heterogeneous population of trimeric holoenzymes, composed of a conserved catalytic subunit and a structural subunit along with a variable regulatory subunit which directs the holoenzyme to a specific target. We now report the identification of a specific PP2A regulatory subunit, B56α, that selectively associates with the N terminus of c-Myc. B56α directs intact PP2A holoenzymes to c-Myc, resulting in a dramatic reduction in c-Myc levels. Inhibition of PP2A-B56α holoenzymes, using small hairpin RNA to knock down B56α, results in c-Myc overexpression, elevated levels of c-Myc serine 62 phosphorylation, and increased c-Myc function. These results uncover a new protein involved in regulating c-Myc expression and reveal a critical interconnection between a potent oncoprotein, c-Myc, and a well-documented tumor suppressor, PP2A.


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