Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism - PubMed (original) (raw)

. 1997 Dec 12;278(5345):1957-60.

doi: 10.1126/science.278.5345.1957.

M Schutkowski, M Shen, X Z Zhou, P T Stukenberg, J U Rahfeld, J Xu, J Kuang, M W Kirschner, G Fischer, L C Cantley, K P Lu

Affiliations

• PMID: 9395400
• DOI: 10.1126/science.278.5345.1957

Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism

M B Yaffe et al. Science. 1997.

Abstract

Pin1 is an essential and conserved mitotic peptidyl-prolyl isomerase (PPIase) that is distinct from members of two other families of conventional PPIases, cyclophilins and FKBPs (FK-506 binding proteins). In response to their phosphorylation during mitosis, Pin1 binds and regulates members of a highly conserved set of proteins that overlaps with antigens recognized by the mitosis-specific monoclonal antibody MPM-2. Pin1 is here shown to be a phosphorylation-dependent PPIase that specifically recognizes the phosphoserine-proline or phosphothreonine-proline bonds present in mitotic phosphoproteins. Both Pin1 and MPM-2 selected similar phosphorylated serine-proline-containing peptides, providing the basis for the specific interaction between Pin1 and MPM-2 antigens. Pin1 preferentially isomerized proline residues preceded by phosphorylated serine or threonine with up to 1300-fold selectivity compared with unphosphorylated peptides. Pin1 may thus regulate mitotic progression by catalyzing sequence-specific and phosphorylation-dependent proline isomerization.

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Comment in

• Pinning down cell division.
  Vogel G. Vogel G. Science. 1997 Dec 12;278(5345):1883-4. doi: 10.1126/science.278.5345.1883. Science. 1997. PMID: 9417635 No abstract available.

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