First-pass extracted concept

human myosin VI

Candidate: toolkit item1 source documents5 linked claims

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Aliases

human full-length myosin VI, myosin VI

Evidence Snippets

LOVDab robustly recruits human full-length myosin VI to various organelles in vivo

Evidence 1Source 1DOI PubMedprovenance

Supporting Sources

Source 1primary paper2017Proceedings of the National Academy of SciencesDOI PubMed

1 evidence snippet 5 linked claims Claim 1 Claim 2 Claim 3

Linked Claims

Claim 1cellular recruitmentsupports2017Source 1DOI PubMed

LOVDab robustly recruits human full-length myosin VI to various organelles in vivo.

Quoted textsource-backed

LOVDab robustly recruits human full-length myosin VI to various organelles in vivo

Claim 2in vitro activationsupports2017Source 1DOI PubMed

LOVDab activates myosin VI in an in vitro gliding filament assay.

Quoted textsource-backed

LOVDab also activates myosin VI in an in vitro gliding filament assay

Claim 3mechanismsupports2017Source 1DOI PubMed

The LOVDab approach harnesses the native targeting and activation mechanism of myosin VI.

Quoted textsource-backed

Our approach harnesses the native targeting and activation mechanism of myosin VI

Claim 4mechanistic inferencesupports2017Source 1DOI PubMed

Protein and lipid cargoes cooperate to activate myosin VI, enabling integration of Ca2+, lipid, and protein cargo signals for site-specific deployment.

Quoted textsource-backed

Our data suggest that protein and lipid cargoes cooperate to activate myosin VI, allowing myosin VI to integrate Ca2+, lipid, and protein cargo signals in the cell to deploy in a site-specific manner.

Claim 5tool creationsupports2017Source 1DOI PubMed

LOVDab is an optogenetic tool created to activate myosin VI by fusing the phototropin1 LOV2 domain to a peptide from Dab2.

Quoted textsource-backed

we created an optogenetic tool for activating myosin VI by fusing the light-sensitive Avena sativa phototropin1 LOV2 domain to a peptide from Dab2 (LOVDab)