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ProteomicsMudPIT analyses of the human proteins biotinylated by proximity to biotin ligase (BioID) fused to the N-terminus of activators of the dynein/dynactin motor
To capture the spatial organization of the dynein/dynactin motor, we attached a promiscuous biotin ligase (BioID) to 6 distinct activators of the dynein machinery motile activity. BioID experiments were performed with stable HEK293 cell lines expressing full length BICD1, BICD2, HOOK1, HOOK3, NIN an...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-30 | MSV000080807 | MassIVE
ProteomicsMudPIT analyses of the human proteins biotinylated by proximity to biotin ligase (BioID) fused to the C-terminus of activators of the dynein/dynactin motor
To understand how a single motor achieves cargo specificity, we attached a promiscuous biotin ligase (BioID) to 6 distinct activators of the dynein machinery motile activity, including two new activators, ninein and ninein-like. BioID experiments were performed with stable HEK293 cell lines expressi...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-30 | MSV000080808 | MassIVE
ProteomicsMudPIT analyses of the human proteins biotinylated by proximity to dynein/dynactin subunits fused to biotin ligase (BioID)
We identified the human dynein proteome by attaching a promiscuous biotin ligase (BioID) to 7 distinct components of the dynein machinery, including a subunit of its essential cofactor dynactin. BioID experiments were performed with stable HEK293 cell lines expressing dynein (IC1, IC2, LIC1, LIC2, R...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080759 | MassIVE
ProteomicsCrosslinking/mass spectrometry (CLMS) analysis of Tetrahymena ODA-Q22MS1 complex
The outer dynein arms (ODAs) are the main force generators in cilia. Crosslinking/mass spectrometry (CLMS) was applied to investigate the interaction between ODA and its binding factor Q22MS1.
ORGANISM(S): Tetrahymena 
2021-12-07 | PXD022936 | JPOST Repository
ProteomicsKIF1A Motor-Neck domain interaction
Quantitative Analysis of Motor-Neck Interaction by the Combination of Protein Painting and Stable Isotope Tags Labelling
ORGANISM(S): Sus Scrofa 
2021-12-23 | PXD026083 | JPOST Repository
ProteomicsHEATR5B associates with dynein-dynactin and selectively promotes motility of AP1- bound endosomal membranes_BioMass@LMB
The dynein motor complex mediates polarised trafficking of a wide variety of organelles, intracellular vesicles and macromolecules. These functions are dependent on the dynactin 5 complex, which helps recruit cargoes to dynein’s tail region and activates motor movement. How dynein and dynactin or...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) Drosophila melanogaster (Fruit fly) 
2023-10-20 | PXD043387 | Pride
Dynein motor complex Dynactin 
ProteomicsRUFY3 links Arl8b and JIP4-Dynein complex to regulate lysosome size and positioning
The whole-cell scale spatial organization of lysosomes is regulated by their bidirectional motility on microtubule tracks. Small GTP-binding (G) protein, Arl8b, stimulates the anterograde transport of lysosomes by recruiting adaptor protein SKIP (also known as PLEKHM2), which in turn couples the mic...
ORGANISM(S): Homo sapiens (Human) 
2022-03-23 | PXD027010 | Pride
Arl8b Lysosome Small gtpase Dynein Microtubule 
TranscriptomicsImmunopurification results of cytoskeletal motor proteins in S. cerevisiae
The accompanying dataset is the result of a systematic study to identify the RNA cargoes associated with the cytoskeletal motor proteins of Saccharomyces cerevisiae. We immunopurified, via the use of integrated, C-terminal GFP and 9Myc tags, the five actomyosin motors, Myo1, Myo2, Myo3, Myo4, and My...
ORGANISM(S): Saccharomyces cerevisiae 
2012-01-27 | E-GEOD-35343 | biostudies-arrayexpress
UnknownDazl can bind to dynein motor complex and may play a role in transport of specific mRNAs.
Not available
S-EPMC1570426 | biostudies-literature
UnknownAnalyses of dynein heavy chain mutations reveal complex interactions between dynein motor domains and cellular dynein functions.
Not available
S-EPMC3415999 | biostudies-literature
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