ArticleOncogene2000
The Adenomatous Polyposis Coli-protein (APC) interacts with the protein tyrosine phosphatase PTP-BL via an alternatively spliced PDZ domain.
Article in Oncogene, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 75 citations in OpenAlex.
- Targeting PTPN13 with 11-amino-acid peptides of C-terminal APC prevents immune evasion of colorectal cancer.Cell research · 2026Article
- The function of alternative splicing in the proteome: rewiring protein interactomes to put old functions into new contexts.Nature structural & molecular biology · 2023Review
- Dual Role of the PTPN13 Tyrosine Phosphatase in Cancer.Biomolecules · 2020Review
- The binding affinity of PTPN13's tandem PDZ2/3 domain is allosterically modulated.BMC molecular and cell biology · 2019Article
- Understanding the effect of alternative splicing in the folding and function of the second PDZ from protein tyrosine phosphatase-BL.Scientific reports · 2015Article
- Protein tyrosine phosphatases as potential therapeutic targets.Acta pharmacologica Sinica · 2014Review
- Downregulation of protein tyrosine phosphatase PTPL1 alters cell cycle and upregulates invasion-related genes in prostate cancer cells.Clinical & experimental metastasis · 2012Article
- The rates of protein synthesis and degradation account for the differential response of neurons to spaced and massed training protocols.PLoS computational biology · 2011Article
- PTPN13/PTPL1: an important regulator of tumor aggressiveness.Anti-cancer agents in medicinal chemistry · 2011Review
- Crystallographic and nuclear magnetic resonance evaluation of the impact of peptide binding to the second PDZ domain of protein tyrosine phosphatase 1E.Biochemistry · 2010Article
- Nuclear APC.Advances in experimental medicine and biology · 2009Review
- Adenomatous polyposis coli (APC) plays multiple roles in the intestinal and colorectal epithelia.Medical molecular morphology · 2007Review
- Subcellular localization and differentiation-induced redistribution of the protein tyrosine phosphatase PTP-BL in Neuroblastoma cells.Cellular and molecular neurobiology · 2005Article
- Redefining the subcellular location and transport of APC: new insights using a panel of antibodies.EMBO reports · 2005Article
- The interaction of PTP-BL PDZ domains with RIL: an enigmatic role for the RIL LIM domain.Molecular biology reports · 2004Article
- Role of APC and DNA mismatch repair genes in the development of colorectal cancers.Molecular cancer · 2003Review
- Interaction of the protein tyrosine phosphatase PTPL1 with the PtdIns(3,4)P2-binding adaptor protein TAPP1.The Biochemical journal · 2003Article
- PDZ domains-glue and guide.Molecular biology reports · 2003Review
- The protein tyrosine phosphatase PTP-BL associates with the midbody and is involved in the regulation of cytokinesis.Molecular biology of the cell · 2003Article
- Cell density and phosphorylation control the subcellular localization of adenomatous polyposis coli protein.Molecular and cellular biology · 2001Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mutations of the tumor suppressor protein APC (Adenomatous Polyposis Coli) are linked to familiar and sporadic human colon cancer. Here we describe a novel interaction between the APC protein and the protein tyrosine phosphatase PTP-BL carrying five PDZ protein-protein interaction domains. Exclusively, the second PDZ domain (PDZ2) of PTP-BL is binding to the extreme C-terminus of the APC protein, as determined by yeast two-hybrid studies. Using surface plasmon resonance analysis we established a dissociation constant (K(D)) of 8.1 x 10(-9) M. We find that a naturally occurring splice insertion of five amino acids (PDZ2b) abolishes its binding affinity to the APC protein. The in vivo interaction between PTP-BL and the APC protein was shown by coprecipitation experiments in transfected COS cells. Furthermore, in cultured epithelial Madine Carnine Kidney cells the subcellular colocalization was demonstrated for the nucleus and also for the tips of cellular extensions. The interaction of the APC protein with a protein tyrosine phosphatase may indirectly modulate the steady state levels of tyrosine phosphorylations of associated proteins, such as beta-catenin playing a major role in the regulation of cell division, migration and cell adhesion.
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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.