{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Fan Y"],"funding":["NCATS NIH HHS","NHLBI NIH HHS"],"pagination":["47-55"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3392929"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["198(1)"],"pubmed_abstract":["Addition of actin monomer (G-actin) to growing actin filaments (F-actin) at the leading edge generates force for cell locomotion. The polymerization reaction and its regulation have been studied in depth. However, the mechanism responsible for transport of G-actin substrate to the cell front is largely unknown; random diffusion, facilitated transport via myosin II contraction, local synthesis as a result of messenger ribonucleic acid localization, or F-actin turnover all might contribute. By tracking a photoactivatable, nonpolymerizable actin mutant, we show vectorial transport of G-actin in live migrating endothelial cells (ECs). Mass spectrometric analysis identified Myo1c, an unconventional F-actin-binding motor protein, as a major G-actin-interacting protein. The cargo-binding tail dom"],"journal":["The Journal of cell biology"],"pubmed_title":["Myo1c facilitates G-actin transport to the leading edge of migrating endothelial cells."],"pmcid":["PMC3392929"],"funding_grant_id":["R01 HL75255","P01 HL76491","P01 HL029582","P01 HL076491","UL1 TR000439","P01 HL29582","R21 HL094841","R01 HL075255"],"pubmed_authors":["Hitomi M","Fan Y","Eswarappa SM","Fox PL"],"additional_accession":[]},"is_claimable":false,"name":"Myo1c facilitates G-actin transport to the leading edge of migrating endothelial cells.","description":"Addition of actin monomer (G-actin) to growing actin filaments (F-actin) at the leading edge generates force for cell locomotion. The polymerization reaction and its regulation have been studied in depth. However, the mechanism responsible for transport of G-actin substrate to the cell front is largely unknown; random diffusion, facilitated transport via myosin II contraction, local synthesis as a result of messenger ribonucleic acid localization, or F-actin turnover all might contribute. By tracking a photoactivatable, nonpolymerizable actin mutant, we show vectorial transport of G-actin in live migrating endothelial cells (ECs). Mass spectrometric analysis identified Myo1c, an unconventional F-actin-binding motor protein, as a major G-actin-interacting protein. The cargo-binding tail dom","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Jul","modification":"2025-05-18T13:06:41.517Z","creation":"2025-05-18T13:06:41.517Z"},"accession":"S-EPMC3392929","cross_references":{"pubmed":["22778278"],"doi":["10.1083/jcb.201111088"]}}