ArticleBMC cell biology2009
Loss of Dictyostelium HSPC300 causes a scar-like phenotype and loss of SCAR protein.
Article in BMC cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed, 14 citations in OpenAlex.
- De novo actin polymerization is required for model Hirano body formation in Dictyostelium.Biology open · 2016Article
- Moving towards a paradigm: common mechanisms of chemotactic signaling in Dictyostelium and mammalian leukocytes.Cellular and molecular life sciences : CMLS · 2014Review
- SCAR/WAVE: A complex issue.Communicative & integrative biology · 2013Article
- SCAR knockouts in Dictyostelium: WASP assumes SCAR's position and upstream regulators in pseudopods.The Journal of cell biology · 2012Article
- Pseudopod growth and evolution during cell movement is controlled through SCAR/WAVE dephosphorylation.Current biology : CB · 2012Article
- SCAR mediates light-induced root elongation in Arabidopsis through photoreceptors and proteasomes.The Plant cell · 2011Article
- The professional phagocyte Dictyostelium discoideum as a model host for bacterial pathogens.Current drug targets · 2011Review
- Article
- SCAR/WAVE is activated at mitosis and drives myosin-independent cytokinesis.Journal of cell science · 2010Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundSCAR/WAVE proteins couple signalling to actin polymerization, and are thus fundamental to the formation of pseudopods and lamellipods. They are controlled as part of a five-membered complex that includes the tiny HSPC300 protein. It is not known why SCAR/WAVE is found in such a large assembly, but in Dictyostelium the four larger subunits have different, clearly delineated functions.
resultsWe have generated Dictyostelium mutants in which the HSPC300 gene is disrupted. As has been seen in other regulatory complex mutants, SCAR is lost in these cells, apparently by a post-translational mechanism, though PIR121 levels do not change. HSPC300 knockouts resemble scar mutants in slow migration, roundness, and lack of large pseudopods. However hspc300-colonies on bacteria are larger and more similar to wild type, suggesting that some SCAR function can survive without HSPC300. We find no evidence for functions of HSPC300 outside the SCAR complex.
conclusionHSPC300 is essential for most SCAR complex functions. The phenotype of HSPC300 knockouts is most similar to mutants in scar, not the other members of the SCAR complex, suggesting that HSPC300 acts most directly on SCAR itself.
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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.