ArticleThe Journal of biological chemistry2010
PTP1B targets the endosomal sorting machinery: dephosphorylation of regulatory sites on the endosomal sorting complex required for transport component STAM2.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed, 1 synthesis or guideline pooled it, 48 citations in OpenAlex.
- Stay in touch with the endoplasmic reticulum.Science China. Life sciences · 2024Pooled it
- Immunotherapeutic implications of negative regulation by protein tyrosine phosphatases in T cells: the emerging cases of PTP1B and TCPTP.Frontiers in medicine · 2024Review
- Myeloid PTP1B deficiency protects against atherosclerosis by improving cholesterol homeostasis through an AMPK-dependent mechanism.Journal of translational medicine · 2023Article
- Reversible phase separation of ESCRT protein ALIX through tyrosine phosphorylation.Science advances · 2023Article
- ER as master regulator of membrane trafficking and organelle function.The Journal of cell biology · 2022Review
- Quantitative proteomics identifies PTP1B as modulator of B cell antigen receptor signaling.Life science alliance · 2021Article
- The functional universe of membrane contact sites.Nature reviews. Molecular cell biology · 2020Review
- ER morphology and endo-lysosomal crosstalk: Functions and disease implications.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020Review
- Article
- Roles for ER:endosome membrane contact sites in ligand-stimulated intraluminal vesicle formation.Biochemical Society transactions · 2018Review
- Membrane dynamics and organelle biogenesis-lipid pipelines and vesicular carriers.BMC biology · 2017Article
- Integrated analysis of proteome, phosphotyrosine-proteome, tyrosine-kinome, and tyrosine-phosphatome in acute myeloid leukemia.Proteomics · 2017Article
- An Endosomal NAADP-Sensitive Two-Pore CaCell reports · 2017Article
- The formation and function of ER-endosome membrane contact sites.Biochimica et biophysica acta · 2016Review
- Allosteric proteins as logarithmic sensors.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Annexin A1 Tethers Membrane Contact Sites that Mediate ER to Endosome Cholesterol Transport.Developmental cell · 2016Article
- UBC9-dependent association between calnexin and protein tyrosine phosphatase 1B (PTP1B) at the endoplasmic reticulum.The Journal of biological chemistry · 2015Article
- Protein-tyrosine phosphatase 1B substrates and metabolic regulation.Seminars in cell & developmental biology · 2015Review
- Superoxide anion radicals induce IGF-1 resistance through concomitant activation of PTP1B and PTEN.EMBO molecular medicine · 2015Article
- Receptor tyrosine kinases endocytosis in endothelium: biology and signaling.Arteriosclerosis, thrombosis, and vascular biology · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Dephosphorylation and endocytic down-regulation are distinct processes that together control the signaling output of a variety of receptor tyrosine kinases (RTKs). PTP1B can directly dephosphorylate several RTKs, but it can also promote activation of downstream pathways through largely unknown mechanisms. These positive signaling functions likely contribute to the tumor-promoting effect of PTP1B in mouse cancer models. Here, we have identified STAM2, an endosomal protein involved in sorting activated RTKs for lysosomal degradation, as a substrate of PTP1B. PTP1B interacts with STAM2 at defined phosphotyrosine sites, and knockdown of PTP1B expression augments STAM2 phosphorylation. Intriguingly, manipulating the expression and phosphorylation state of STAM2 did not have a general effect on epidermal growth factor (EGF)-induced EGF receptor trafficking, degradation, or signaling. Instead, phosphorylated STAM2 specifically suppressed Akt activation, and a phosphorylation-deficient STAM2 mutant displayed prolonged localization on endosomes following EGF stimulation. These results reveal a novel link between the dephosphorylation and endocytic machinery and suggest that PTP1B can affect RTK signaling in a previously unrecognized manner.
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Identifiers
What OpenQuestion holds
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.