ArticleMolecular and cellular biology1994
Nuclear localization of the PEP protein tyrosine phosphatase.
Article in Molecular and cellular biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 31 citations in OpenAlex.
- SHP2 as a primordial epigenetic enzyme expunges histone H3 pTyr-54 to amend androgen receptor homeostasis.Nature communications · 2024Article
- ER Stress, CREB, and Memory: A Tangled Emerging Link in Disease.The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry · 2019Review
- Tyrosine phosphatase PTPN22: multifunctional regulator of immune signaling, development, and disease.Annual review of immunology · 2014Review
- The tumor-suppressor activity of PTEN is regulated by its carboxyl-terminal region.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- PSTPIP: a tyrosine phosphorylated cleavage furrow-associated protein that is a substrate for a PEST tyrosine phosphatase.The Journal of cell biology · 1997Article
- STEP61: a member of a family of brain-enriched PTPs is localized to the endoplasmic reticulum.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1996Article
- Association of inhibitory tyrosine protein kinase p50csk with protein tyrosine phosphatase PEP in T cells and other hemopoietic cells.The EMBO journal · 1996Article
- Murine protein tyrosine phosphatase-PEST, a stable cytosolic protein tyrosine phosphatase.The Biochemical journal · 1995Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PEP is an intracellular protein tyrosine phosphatase expressed primarily by cells of hematopoietic origin that can be divided structurally into a catalytic domain and a large carboxy-terminal domain. The carboxy-terminal domain is enriched in proline, glutamic acid, serine, and threonine residues (PEST sequences) and contains a nonperfect tandem repeat sequence enriched in proline residues and a carboxy terminus enriched in basic amino acids. Here we show that PEP is diffusely expressed in lymphoid tissues, consistent with expression by many different cell types. Analysis of the PEP protein identifies a nuclear localization sequence within the extreme carboxy terminus. Transfer of 18 amino acids from the carboxy terminus of PEP to beta-galactosidase conferred nuclear localization, indicating that this sequence was sufficient for nuclear localization. Proteins enriched in PEST sequences are often rapidly degraded. However, pulse-chase analysis indicates that PEP has a half-life of greater than 5 h.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.