ArticleMolecular biology of the cell1998
Tyrosine phosphorylation of selected secretory carrier membrane proteins, SCAMP1 and SCAMP3, and association with the EGF receptor.
Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Secretory carrier membrane protein 3 modulates nuclear ERK1/2 signaling and drug response in triple-negative breast cancer.Frontiers in oncology · 2026Article
- Optimized Proteomic Analysis of Insulin Granules From MIN6 Cells Identifies Scamp3, a Novel Regulator of Insulin Secretion and Content.Diabetes · 2024Article
- SCAMP1 silencing inhibits proliferation by attenuating multiple pro-survival signaling pathways in gastric cancer.Journal of Cancer · 2024Article
- Article
- SCAMP2/5 as diagnostic and prognostic markers for acute myeloid leukemia.Scientific reports · 2021Article
- SCAMP3 is a mutant EGFR phosphorylation target and a tumor suppressor in lung adenocarcinoma.Oncogene · 2021Article
- SCAMP5 mediates activity-dependent enhancement of NHE6 recruitment to synaptic vesicles during synaptic plasticity.Molecular brain · 2021Article
- SCAMP3 Promotes Glioma Proliferation and Indicates Unfavorable Prognosis via Multiple Pathways.OncoTargets and therapy · 2020Article
- Molecular mechanisms of OLIG2 transcription factor in brain cancer.Oncotarget · 2016Article
- Genetic regulation of sex differences in songbirds and lizards.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016Review
- SCAMP5 plays a critical role in synaptic vesicle endocytosis during high neuronal activity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- Inhibition of SCAMP1 suppresses cell migration and invasion in human pancreatic and gallbladder cancer cells.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2013Article
- Secretory carrier membrane proteins.Protoplasma · 2012Review
- Hepatitis C virus network based classification of hepatocellular cirrhosis and carcinoma.PloS one · 2012Article
- A mobile secretory vesicle cluster involved in mass transport from the Golgi to the plant cell exterior.The Plant cell · 2009Article
- SCAMP3 negatively regulates epidermal growth factor receptor degradation and promotes receptor recycling.Molecular biology of the cell · 2009Article
- Detailed characterization of the mouse embryonic stem cell transcriptome reveals novel genes and intergenic splicing associated with pluripotency.BMC genomics · 2008Article
- Sexually dimorphic SCAMP1 expression in the forebrain motor pathway for song production of juvenile zebra finches.Developmental neurobiology · 2007Article
- Medullary cystic kidney disease type 1: mutational analysis in 37 genes based on haplotype sharing.Human genetics · 2006Article
- Role of secretory carrier membrane protein SCAMP2 in granule exocytosis.Molecular biology of the cell · 2002Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Secretory carrier membrane proteins (SCAMPs) are ubiquitously expressed proteins of post-Golgi vesicles. In the presence of the tyrosine phosphatase inhibitor vanadate, or after overexpression in Chinese hamster ovary (CHO) cells, SCAMP1 and SCAMP3 are phosphorylated selectively on tyrosine residue(s). Phosphorylation is reversible after vanadate washout in situ or when isolated SCAMP3 is incubated with the recombinant tyrosine phosphatase PTP1B. Vanadate also causes the partial accumulation of SCAMP3, but not SCAMP1, in "patches" at or near the cell surface. A search for SCAMP kinase activities has shown that SCAMPs 1 and 3, but not SCAMP2, are tyrosine phosphorylated in EGF-stimulated murine fibroblasts overexpressing the EGF receptor (EGFR). EGF catalyzes the progressive phosphorylation of the SCAMPs up to 1 h poststimulation and may enhance colocalization of the EGFR and SCAMP3 within the cell interior. EGF also induces SCAMP-EGFR association, as detected by coimmunoprecipitation, and phosphorylation of SCAMP3 is stimulated by the EGFR in vitro. These results suggest that phosphorylation of SCAMPs, either directly or indirectly, may be functionally linked to the internalization/down-regulation of the EGFR.
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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.