The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Sequence-Specific and Phosphorylation-Dependent Proline Isomerization: A Potential Mitotic Regulatory Mechanism
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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Cites
Chemistry and Biology of the Immunophilins and Their Immunosuppressive Ligands
Schreiber, S. L. (1991) · Science · doi:10.1126/science.1702904 · Cited by 1,494
Blangy, A., Lane, H. A., d'Hérin, P., Harper, M., Kress, M., & Niggt, E. A. (1995) · Cell · doi:10.1016/0092-8674(95)90142-6 · Cited by 952
Cited by
Signaling Through Scaffold, Anchoring, and Adaptor Proteins
Pawson, T., & Scott, J. D. (1997) · Science · doi:10.1126/science.278.5346.2075 · Cited by 2,256
The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein
Lu, P.-J., Wulf, G., Zhou, X. Z., Davies, P., & Lu, K. P. (1999) · Nature · doi:10.1038/21650 · Cited by 721
Self-citationThe prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease
Lu, K. P., & Zhou, X. Z. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2261 · Cited by 682
Self-citationLi, X., Jiang, Y., Meisenhelder, J., Yang, W., Hawke, D. H., Zheng, Y., Xia, Y., Aldape, K., He, J., Hunter, T., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.009 · Cited by 508
The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-β production
Pastorino, L., Sun, A., Lu, P.-J., Zhou, X. Z., Balastik, M., Finn, G., Wulf, G., Lim, J., Li, S.-H., Li, X., et al. (2006) · Nature · doi:10.1038/nature04543 · Cited by 487
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Metadata
- Authors
- Yaffe, M. B., Schutkowski, M., Shen, M., Zhou, X. Z., Stukenberg, P. T., Rahfeld, J.-U., Xu, J., Kuang, J., Kirschner, M. W., Fischer, G., Cantley, L. C., & Lu, K. P.
- Venue
- Science
- Published
- 1997-12-12
- Volume
- 278
- Issue
- 5345
- Pages
- 1957-1960
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2126043496
- Cited by
- 770
- References
- 2
- FWCI
- 8.32
- Type
- journal article
- Language
- en
- Open access
- closed
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- The paper
- Yaffe, M. B., Schutkowski, M., Shen, M., Zhou, X. Z., Stukenberg, P. T., Rahfeld, J.-U., Xu, J., Kuang, J., Kirschner, M. W., Fischer, G., Cantley, L. C., & Lu, K. P. (1997). Sequence-Specific and Phosphorylation-Dependent Proline Isomerization: A Potential Mitotic Regulatory Mechanism. Science. https://doi.org/10.1126/science.278.5345.1957
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