{"doi":"10.1016/j.bpj.2015.11.3302","title":"Myosin 19 is an Outer Mitochondrial Membrane Motor and Effector of Starvation Induced Filopodia with Unique Kinetic Features","abstract":null,"journal":"Biophysical Journal","year":2016,"id":674678,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":0,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1095430,"name":"Boris Shneyer","orcid":null,"position":1,"is_corresponding":false},{"id":1762773,"name":"Marko Usaj","orcid":null,"position":2,"is_corresponding":false},{"id":1762772,"name":"Arnon Henn","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Myosin 19 is an Outer Mitochondrial Membrane Motor and Effector of Starvation Induced Filopodia with Unique Kinetic Features","abstract":"The interaction between the actin cytoskeleton, myosin motors and their function in mitochondria dynamics, morphology and cellular localization is now beginning to emerge. A novel function for actin-based motors as regulators of cellular adaptations to stress, linking actin cytoskeleton remodelling to mitochondria dynamics. We reveal a novel function for myosin 19 in mitochondrial dynamics and localization during cellular response to glucose starvation. Ectopically expressed myosin 19 localizes with mitochondria at the tips of starvation-induced filopodia. Corollary to this, RNAi mediated knockdown of myosin 19 diminished their formation without evident effects on the mitochondrial network. We analyzed myosin 19 mitochondria interaction and demonstrated that it is uniquely anchored to the outer mitochondrial membrane (OMM) via a 30-residue motif, indicating that myosin 19 is a stably attached OMM molecular motor. To this end, we have purified myosin 19-3IQ motor domain construct. Myosin 19-3IQ featured characteristic actin-activated ATPase activity with moderate to slow turnover (kcat) and relatively tight KATPase. Our transient kinetics and steady state equilibrium binding experiments revealed that myosin 19-3IQ binds ATP and ADP with tight affinity that, to the best of our knowledge, have not yet been exhibited by any other myosins. We suspect that this feature allows myosin 19 to operate in a unique cellular environment that may be related to cellular stress conditions as we showed in our previous studies. The detailed knowledge of myosin 19 enzymatic adaptation will provide us with a quantitative working model of myosin 19, and will assist us to understand its cellular function. Our work reveals a novel function for myosin 19 in mitochondrial positioning during homeostasis and under stress conditions and broadens our understanding of the actin cytoskeleton- myosin -mitochondria interplay.","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"19162232","pmcid":null,"openalex_id":"https://openalex.org/W2509291357","authors":[],"funders":[{"funder_name":"National Institutes of Health","grant_id":"9R01GM086352-28","title":"Structural Dynamics Of Actomyosin Motility"},{"funder_name":"National Institutes of Health","grant_id":"5T32HL007954-10","title":"Multidisciplinary training in cardiovascular biology"}],"total_grants":2,"fwci":0.0,"citation_percentile":0.13120277,"influential_citations":0,"citation_trend":[],"oa_status":"bronze","license":"Elsevier Non-Commercial","oa_locations":[{"url":"http://www.cell.com/article/S0006349515044859/pdf","host_type":"journal"},{"url":"http://www.cell.com/article/S0006349515044859/pdf","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0006349515044859?httpAccept=text/plain","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0006349515044859?httpAccept=text/xml","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.bpj.2015.11.3302","host_type":"journal"},{"url":"http://dx.doi.org/10.1016/j.bpj.2015.11.3302","host_type":""},{"url":"https://dx.doi.org/10.1016/j.bpj.2015.11.3302","host_type":""}],"fields_of_study":["Cardiomyopathy and Myosin Studies","Mitochondrial Function and Pathology","RNA Research and Splicing","0301 basic medicine","0303 health sciences","03 medical and health sciences"],"mesh_terms":[],"keywords":["Myosin","Filopodia","Actin","Mitochondrion","Cell biology","Biology","Motor protein","Molecular motor","Cytoskeleton","Actin cytoskeleton","Biochemistry","Biophysics","Cell","Microtubule"],"sdg_mappings":[{"sdg_number":1,"sdg_label":"1. No poverty"},{"sdg_number":2,"sdg_label":"2. Zero hunger"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-16T17:45:45.514341Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}