ArticleMolecular and cellular biology1998
Identification of major binding proteins and substrates for the SH2-containing protein tyrosine phosphatase SHP-1 in macrophages.
Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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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.
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Who cites it
66 citing papers in PubMed, 198 citations in OpenAlex.
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- CD47-mediated tumor microenvironment remodeling: a central mechanism in immune evasion.Acta biochimica et biophysica Sinica · 2025Review
- A pan-allelic human SIRPα-blocking antibody, ES004-B5, promotes tumor killing by enhancing macrophage phagocytosis and subsequently inducing an effective T-cell response.Antibody therapeutics · 2024Article
- A Perspective on the CD47-SIRPA Axis in High-Risk Neuroblastoma.Current oncology (Toronto, Ont.) · 2024Review
- SHP-1 inhibition targets leukaemia stem cells to restore immunosurveillance and enhance chemosensitivity by metabolic reprogramming.Nature cell biology · 2024Article
- Loss of Shp1 impairs myeloid cell function and causes lethal inflammation in zebrafish larvae.Disease models & mechanisms · 2023Article
- On the relationship between extant innate immune receptors and the evolutionary origins of jawed vertebrate adaptive immunity.Immunogenetics · 2022Review
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- The complex interactions between the cellular and non-cellular components of the brain tumor microenvironmental landscape and their therapeutic implications.Frontiers in oncology · 2022Review
- Macrophage-Based Combination Therapies as a New Strategy for Cancer Immunotherapy.Kidney diseases (Basel, Switzerland) · 2022Review
- Putting the brakes on phagocytosis: "don't-eat-me" signaling in physiology and disease.EMBO reports · 2021Review
- PRRG4 promotes breast cancer metastasis through the recruitment of NEDD4 and downregulation of Robo1.Oncogene · 2020Article
- Targeting macrophage checkpoint inhibitor SIRPα for anticancer therapy.JCI insight · 2020Article
- Restoration of miR-340 controls pancreatic cancer cellJournal for immunotherapy of cancer · 2020Article
- The Role of Microglia in Glioblastoma.Frontiers in oncology · 2020Review
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- Signal regulatory protein α protects podocytes through promoting autophagic activity.JCI insight · 2019Article
- Targeting the CD47-SIRPα signaling axis: current studies on B-cell lymphoma immunotherapy.The Journal of international medical research · 2018Review
- Tyrosine phosphorylation of the transmembrane protein SIRPα: Sensing synaptic activity and regulating ectodomain cleavage for synapse maturation.The Journal of biological chemistry · 2018Article
6 more citing papers are in PubMed but not listed here.
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
The protein tyrosine phosphatase SHP-1 is a critical regulator of macrophage biology, but its detailed mechanism of action remains largely undefined. SHP-1 associates with a 130-kDa tyrosyl-phosphorylated species (P130) in macrophages, suggesting that P130 might be an SHP-1 regulator and/or substrate. Here we show that P130 consists of two transmembrane glycoproteins, which we identify as PIR-B/p91A and the signal-regulatory protein (SIRP) family member BIT. These proteins also form separate complexes with SHP-2. BIT, but not PIR-B, is in a complex with the colony-stimulating factor 1 receptor (CSF-1R), suggesting that BIT may direct SHP-1 to the CSF-1R. BIT and PIR-B bind preferentially to substrate-trapping mutants of SHP-1 and are hyperphosphorylated in macrophages from motheaten viable mice, which express catalytically impaired forms of SHP-1, indicating that these proteins are SHP-1 substrates. However, BIT and PIR-B are hypophosphorylated in motheaten macrophages, which completely lack SHP-1 expression. These data suggest a model in which SHP-1 dephosphorylates specific sites on BIT and PIR-B while protecting other sites from dephosphorylation via its SH2 domains. Finally, BIT and PIR-B associate with two tyrosyl phosphoproteins and a tyrosine kinase activity. Tyrosyl phosphorylation of these proteins and the level of the associated kinase activity are increased in the absence of SHP-1. Our data suggest that BIT and PIR-B recruit multiple signaling molecules to receptor complexes, where they are regulated by SHP-1 and/or SHP-2.
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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.