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Gene Review

RRD2  -  peptidylprolyl isomerase RRD2

Saccharomyces cerevisiae S288c

Synonyms: NOH1, PPIase PTPA-2, Peptidyl-prolyl cis-trans isomerase PTPA-2, Phosphotyrosyl phosphatase activator 2, Rotamase PTPA-2, ...
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High impact information on RRD2

  • We present here the crystal structures of human PTPA and of the two yeast orthologs (Ypa1 and Ypa2), revealing an all alpha-helical protein fold that is radically different from other PPIases [1].
  • Ypa1 interacts specifically with Pph3, Sit4 and Ppg1, whereas Ypa2 binds to Pph21 and Pph22 [2].
  • The Ypa1 and Ypa2 proteins do not compete with Tap42 (PP2A associating protein) for binding to PP2A family members [2].

Biological context of RRD2


Regulatory relationships of RRD2

  • Strikingly, the interaction of Ypa2 with yeast PP2A is promoted by the presence of Ypa1, suggesting a positive role of Ypa1 in the regulation of PP2A association with other interacting proteins [2].

Other interactions of RRD2

  • Strains lacking both NCS1 and NOH1 were inviable and arrested as unbudded cells, implying that PTPA function is required for proper G(1) progression [4].


  1. Crystal structure of the PP2A phosphatase activator: implications for its PP2A-specific PPIase activity. Leulliot, N., Vicentini, G., Jordens, J., Quevillon-Cheruel, S., Schiltz, M., Barford, D., van Tilbeurgh, H., Goris, J. Mol. Cell (2006) [Pubmed]
  2. Specific interactions of PP2A and PP2A-like phosphatases with the yeast PTPA homologues, Ypa1 and Ypa2. Van Hoof, C., Martens, E., Longin, S., Jordens, J., Stevens, I., Janssens, V., Goris, J. Biochem. J. (2005) [Pubmed]
  3. Functional analysis of RRD1 (YIL153w) and RRD2 (YPL152w), which encode two putative activators of the phosphotyrosyl phosphatase activity of PP2A in Saccharomyces cerevisiae. Rempola, B., Kaniak, A., Migdalski, A., Rytka, J., Slonimski, P.P., di Rago, J.P. Mol. Gen. Genet. (2000) [Pubmed]
  4. The phosphotyrosyl phosphatase activator, Ncs1p (Rrd1p), functions with Cla4p to regulate the G(2)/M transition in Saccharomyces cerevisiae. Mitchell, D.A., Sprague, G.F. Mol. Cell. Biol. (2001) [Pubmed]
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