PXD015004 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | MYO19 interacts weakly with Miro2 GTPases on the mitochondrial outer membrane |
Description | MYO19 interacts with mitochondria through a unique C-terminal mitochondrial association domain (MyMOMA). The specific molecular mechanisms for localization of MYO19 to mitochondria are poorly understood. Using promiscuous biotinylation, we have identified ~100 candidate MYO19 interacting proteins, a subset of which were also identified in via affinity-capture experiments. We chose to further explore the interaction between MYO19 and the mitochondrial GTPase Miro2 by expressing mchr-Miro2 in combination with GFP-tagged fragments of the MyMOMA domain and assaying for recruitment of MYO19-GFP to mitochondria. Co-expression of MYO19898-970-GFP with mchr-Miro2 enhanced MYO19898-970-GFP localization to mitochondria. Mislocalizing Miro2 to filopodial tips or the cytosolic face of the nuclear envelope did not recruit MYO19898-970-GFP to either location. To address the kinetics of the Miro2/MYO19 interaction, we used FRAP analysis and permeabilization-activated reduction in fluorescence (PARF) analysis. MyMOMA constructs containing a putative membrane insertion motif but lacking the complete Miro2 interacting region, MYO19853-935-GFP, displayed slow exchange kinetics. MYO19898-970-GFP, which does not include the membrane-insertion motif, displayed rapid exchange kinetics, suggesting that the MYO19 and Miro2 interaction is weaker than between MYO19 and the mitochondrial outer membrane. Mutation of well-conserved, charged residues within MYO19 or within the switch I and II regions of Miro2 abolished the enhancement of MYO19898-970-GFP localization in cells ectopically expressing mchr-Miro2. Additionally, expressing mutant versions of Miro2 thought to represent particular nucleotide states indicated that the enhancement of MYO19898-970-GFP localization is dependent on Miro2 nucleotide state. Taken together, these data suggest a role for Miro2 in regulation and integration of actin- and microtubule-based mitochondrial activities. |
HostingRepository | PRIDE |
AnnounceDate | 2019-09-11 |
AnnouncementXML | Submission_2019-09-11_05:58:01.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Omar Quintero |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | No PTMs are included in the dataset |
Instrument | Orbitrap Fusion Lumos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2019-08-13 01:14:09 | ID requested | |
⏵ 1 | 2019-09-11 05:58:03 | announced | |
Publication List
Bocanegra JL, Fujita BM, Melton NR, Cowan JM, Schinski EL, Tamir TY, Major MB, Quintero OA, The MyMOMA domain of MYO19 encodes for distinct Miro-dependent and Miro-independent mechanisms of interaction with mitochondrial membranes. Cytoskeleton (Hoboken), 77(3-4):149-166(2020) [pubmed] |
Keyword List
submitter keyword: MYO19, mitochondria, HeLa, BioID2, APMS |
Contact List
Omar A. Quintero |
contact affiliation | Department of Biology, University of Richmond, Richmond, VA |
contact email | oquinter@richmond.edu |
lab head | |
Omar Quintero |
contact affiliation | University of Richmond |
contact email | oquinter@richmond.edu |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/09/PXD015004 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD015004
- Label: PRIDE project
- Name: MYO19 interacts weakly with Miro2 GTPases on the mitochondrial outer membrane