<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Fan Y</submitter><funding>NCATS NIH HHS</funding><funding>NHLBI NIH HHS</funding><pagination>47-55</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3392929</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>198(1)</volume><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</pubmed_abstract><journal>The Journal of cell biology</journal><pubmed_title>Myo1c facilitates G-actin transport to the leading edge of migrating endothelial cells.</pubmed_title><pmcid>PMC3392929</pmcid><funding_grant_id>R01 HL75255</funding_grant_id><funding_grant_id>P01 HL76491</funding_grant_id><funding_grant_id>P01 HL029582</funding_grant_id><funding_grant_id>P01 HL076491</funding_grant_id><funding_grant_id>UL1 TR000439</funding_grant_id><funding_grant_id>P01 HL29582</funding_grant_id><funding_grant_id>R21 HL094841</funding_grant_id><funding_grant_id>R01 HL075255</funding_grant_id><pubmed_authors>Hitomi M</pubmed_authors><pubmed_authors>Fan Y</pubmed_authors><pubmed_authors>Eswarappa SM</pubmed_authors><pubmed_authors>Fox PL</pubmed_authors></additional><is_claimable>false</is_claimable><name>Myo1c facilitates G-actin transport to the leading edge of migrating endothelial cells.</name><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</description><dates><release>2012-01-01T00:00:00Z</release><publication>2012 Jul</publication><modification>2025-05-18T13:06:41.517Z</modification><creation>2025-05-18T13:06:41.517Z</creation></dates><accession>S-EPMC3392929</accession><cross_references><pubmed>22778278</pubmed><doi>10.1083/jcb.201111088</doi></cross_references></HashMap>