ArticleOncogene2002
Light Chain 3 associates with a Sos1 guanine nucleotide exchange factor: its significance in the Sos1-mediated Rac1 signaling leading to membrane ruffling.
Article in Oncogene, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
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- High levels of DEPDC1B predict shorter biochemical recurrence-free survival of patients with prostate cancer.Oncology letters · 2017Article
- Atg8 is involved in endosomal and phagosomal acidification in the parasitic protist Entamoeba histolytica.Cellular microbiology · 2015Article
- Distribution, cleavage and lipidation of Atg8 fusion proteins in Spodoptera litura Sl-HP cells.PloS one · 2014Article
- The actin cytoskeleton participates in the early events of autophagosome formation upon starvation induced autophagy.Autophagy · 2012Article
- Mammalian son of sevenless Guanine nucleotide exchange factors: old concepts and new perspectives.Genes & cancer · 2011Article
- Article
- The ubiquitin-like protein LC3 regulates the Rho-GEF activity of AKAP-Lbc.The Journal of biological chemistry · 2009Article
- Processing of a pestivirus protein by a cellular protease specific for light chain 3 of microtubule-associated proteins.Journal of virology · 2004Article
- Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A 19 kDa protein was identified to associate with the Dbl oncogene homology domain of Sos1 (Sos-DH) and was purified from rat brains by GST-Sos-DH affinity chromatography. Peptide sequencing revealed that the protein is identical to light chain 3 (LC3), a microtubule-associated protein. LC3 coimmunoprecipitated with Sos1, and GST-LC3 was capable of forming complexes with Sos1 in in vitro GST-pull down assay. Furthermore, LC3 was colocalized with Sos1 in cells, as determined by immunohistochemistry. While Sos1 stimulated the guanine nucleotide exchange reaction on Rac1, LC3 suppressed the ability of Sos1 to activate Rac1 in in vitro experiments using COS cell lysates. Consistent with this, overexpression of LC3 decreased the level of active GTP-bound Rac1 in COS cells. Sos1 expression induced membrane ruffling, a downstream target for Rac1, but LC3 expression inhibited this biological effect of Sos1. These findings suggest that LC3 interacts with Sos1 and thereby negatively regulates the Sos1-dependent Rac1 activation leading to membrane ruffling.
Indexed as
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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.