| 2000 |
Myr4 (MYO1D) functions as an actin-based mechanoenzyme required for membrane trafficking along the recycling endosome pathway in MDCK epithelial cells. In vitro assays demonstrated that transfer of endocytosed markers from early endosomes to recycling endosomes depends on myr4 activity, its light chain calmodulin (CaM), and polymerized actin. |
In vitro endosomal transfer assay with functional perturbation of CaM and actin dynamics; identification of myr4 as CaM target protein |
Traffic (Copenhagen, Denmark) |
Medium |
11208135
|
| 2015 |
Myo1D is required for planar cell polarity (PCP) in multi-ciliated tracheal and ependymal epithelial cells. In Myo1d knockout rats, rotational PCP of tracheal cilia is lost, cilia beat in a disordered pattern, and the asymmetric localization of PCP core protein Vangl1 is abolished. In ependymal cells, left-right positioning of basal body clusters is disrupted. Myo1d localizes to the F-actin and basal body-rich subapical cortex of ciliated tracheal cells. |
Knockout rat model (Myo1d KO), scanning and transmission electron microscopy, immunofluorescence localization, bead transport assays |
Cytoskeleton (Hoboken, N.J.) |
High |
26446290
|
| 2015 |
Myo1D (Drosophila) functions with Nesprin1 (dNesp1) to direct mRNA transport from muscle nuclei to postsynaptic sites at the neuromuscular junction. Both dNesp1 and Myo1D are mutually required for their localization to immature boutons along F-actin-based 'railroad tracks.' |
Drosophila genetic analysis, fluorescence imaging of mRNA localization and protein co-localization, mutual requirement demonstrated by loss-of-function |
Neuron |
Medium |
25959729
|
| 2018 |
Myosin1D (Myo1D) is an evolutionarily conserved regulator of left-right asymmetry. In zebrafish, Myo1D controls the formation and function of the left-right organizer (Kupffer's vesicle), regulates cilia orientation, and functionally interacts with the planar cell polarity pathway component VanGogh-like2 (Vangl2) to shape directional fluid flow for symmetry breaking. |
Zebrafish myo1d loss-of-function, genetic epistasis with vangl2, cilia orientation analysis, LRO flow measurements |
Nature communications |
High |
29769531
|
| 2018 |
Myo1D is required for left-right axis formation in Xenopus. Morpholino-mediated myo1d knockdown disrupts organ laterality, impairs flow at the LR organizer through shorter, fewer, and non-polarized cilia, and inhibits convergent extension downstream of Wnt/PCP signaling. Genetic interaction between myo1d and vangl2 was demonstrated. |
Xenopus morpholino knockdown, organ placement scoring, Nodal cascade expression analysis, cilia imaging, gastrula explant convergent extension assay, ATF2 reporter for non-canonical Wnt, genetic epistasis with vangl2 |
Current biology : CB |
High |
29478852
|
| 2019 |
MYO1D anchors unphosphorylated EGFR family members (EGFR, ErbB2, ErbB4, but not ErbB3) to the plasma membrane by binding their kinase domains via a C-terminal β-meander motif in the MYO1D tail domain. MYO1D tethers these receptors to the underlying actin cytoskeleton before ligand activation. Overexpressed MYO1D increases EGFR levels, promotes cancer cell motility and viability, and drives colorectal tumor progression in a syngeneic mouse model. |
Co-immunoprecipitation, co-localization studies, domain-deletion/mutagenesis of MYO1D tail, functional phenotype assays (cell motility, viability), syngeneic mouse tumor model |
Oncogene |
High |
31420606
|
| 2012 |
Myosin-1d interacts with and is co-expressed with aspartoacylase in the nervous system. Myosin-1d localizes along axons and in the myelin compartment of the mouse sciatic nerve, and is enriched in Purkinje and granule cell layers of cerebellum, expanding to myelinated axonal tracts upon onset of myelination. |
Co-immunoprecipitation (interaction with aspartoacylase), immunofluorescence localization in tissue sections |
Brain research |
Low |
22284616
|
| 2014 |
Myo1d is expressed in myelinating oligodendrocytes in the CNS, localizing to abaxonal and adaxonal (outer and inner cytoplasm-containing loop) regions of myelin. Expression increases during myelinogenesis and continues into adulthood. |
Immunohistochemistry with isoform-specific antibody, Western blot fractionation of myelin |
Journal of neuroscience research |
Low |
24903835
|
| 2016 |
Myo1d knockdown in cultured oligodendrocytes causes retraction of processes, degeneration of myelin-like membrane, apoptosis, and impairs intracellular transport of myelin proteolipid protein (PLP). Myo1d localizes at the leading edge of myelin-like membrane, colocalizing with actin filaments, CNPase, and partially with PLP. |
siRNA knockdown, immunofluorescence colocalization, morphological analysis, PLP transport assay in cultured oligodendrocytes |
ASN neuro |
Medium |
27655972
|
| 2017 |
Myo1d knockdown in vivo during remyelination after cuprizone-induced demyelination decreases myelin basic protein and PLP levels, increases pro-inflammatory microglia and astrocytes, decreases anti-inflammatory microglia, and increases caspase-3-positive oligodendrocytes, indicating Myo1d is required for the remyelination process and oligodendrocyte survival. |
In vivo siRNA injection via stereotaxy in cuprizone demyelination mouse model, immunofluorescence, cell counting |
Neurochemical research |
Medium |
28986688
|
| 2022 |
SPAG6 interacts with MYO1D (demonstrated by immunoprecipitation and mass spectrometry). Overexpression of SPAG6 promotes translocation of MYO1D from cytosol to the cell membrane, thereby upregulating EGFR family expression and activating PI3K/AKT and ERK signaling to promote AML cell proliferation and migration. |
Co-immunoprecipitation, mass spectrometry, subcellular fractionation, overexpression and knockdown functional assays, xenograft mouse model |
Blood advances |
Medium |
35667090
|
| 2020 |
In Drosophila, Myo1D is required for the membrane localization of the initiator caspase Dronc in mature enterocytes. In Myo1d mutant midguts, apoptosis-induced proliferation (AiP) signals including ROS generation, hemocyte recruitment, and JNK signaling are impaired, and intestinal stem cell mitotic activity is reduced. |
Drosophila myo1d mutant analysis, live imaging of Dronc membrane localization, ROS detection, JNK reporter assay, hemocyte recruitment scoring, ISC mitosis quantification |
Cell reports |
High |
33238125
|
| 2022 |
In Drosophila, F-actin remodeling driven by LIMK1 acts downstream of the caspase Dronc and depends on Myo1D to mediate ROS production and JNK activation during apoptosis-induced proliferation (AiP). Synergistic effects of Dronc and LIMK1 co-expression on F-actin accumulation, ROS, and JNK activation are abolished in myo1d mutants, placing Myo1D as a required mediator in the Dronc-LIMK1-F-actin-ROS-JNK axis. |
Drosophila genetic epistasis (myo1d mutant background), LIMK1/cofilin overexpression and knockdown, ROS detection, JNK reporter assay, F-actin staining |
PLoS genetics |
High |
36469525
|
| 2023 |
Drosophila Myo1D has distinct ATPase kinetics compared to Myo1C: a 12.5-fold higher actin-activated steady-state ATPase rate, 8-fold higher MgADP release rate, and rate-limiting step is MgADP release (vs. phosphate release for Myo1C). Myo1D propels actin filaments at higher speeds than Myo1C in in vitro gliding assays and robustly transports 50 nm unilamellar vesicles along actin filaments, while Myo1C does not support vesicle transport. |
Transient kinetic assays (ATPase mechanism determination), in vitro actin gliding assay, in vitro vesicle transport assay |
The Journal of biological chemistry |
High |
37380077
|
| 2024 |
Drosophila Myo1D (but not Myo1C) exhibits a higher proportion of fast-diffusing molecules on the plasma membrane of macrophages, as measured by single-molecule imaging. This distinct membrane diffusion behavior depends on both head and tail domains of each myosin and does not exert mutual influence between paralogs. Myo1D's unique membrane dynamics may underlie its role in dextral cell chirality. |
Single-molecule imaging on Drosophila macrophage plasma membrane, diffusion analysis |
Genes to cells : devoted to molecular & cellular mechanisms |
Medium |
38454557
|
| 2025 |
MYO1D preferentially binds PDGFRα/β heterodimers. Knockdown of MYO1D leads to retention of PDGFRα/β heterodimers at the plasma membrane, resulting in increased ERK1/2 phosphorylation and increased cell proliferation, indicating MYO1D normally promotes PDGFRα/β heterodimer internalization away from the plasma membrane to limit ERK signaling. |
PDGFR dimer-specific interactome (bimolecular fluorescence complementation + proteomics), siRNA knockdown of MYO1D, receptor internalization imaging, ERK1/2 phosphorylation assay, proliferation assay |
Nature communications |
High |
40404618
|
| 2025 |
In Drosophila macrophages, Myo1D directs clockwise circumferential F-actin flow, while Myo1C directs counterclockwise flow; both depend on Myosin2 (Myo2). In a modified in vitro motility assay at near-physiological actin concentrations, Myo1D triggers self-organization of a clockwise-rotating chiral F-actin ring with parallel, annular barbed-end polarity, whereas Myo1C induces random F-actin flow. This provides a molecular basis for how Myo1D establishes dextral cell and organ chirality. |
Live imaging of F-actin flow in Drosophila macrophages, in vitro motility assay with near-physiological actin concentrations, genetic perturbation of Myo2 |
bioRxivpreprint |
Medium |
bio_10.1101_2025.05.06.648335
|
| 2009 |
Xenopus laevis Myo1D (XlMyo1d) protein is present in eggs and increases at early neurula through tadpole stages. mRNA is expressed in neural tube, pre-somitic mesoderm, somites, and cranial neural crest cells during migration; during somitogenesis, transcript localizes to a stripe overlapping the nuclear region of somites. A novel isoform-specific tail homology embedded within the TH1 domain was identified by sequence analysis. |
Western blot (developmental expression), whole-mount in situ hybridization (mRNA localization), sequence analysis |
Development, growth & differentiation |
Low |
19382939
|
| 2025 |
In Drosophila, Myo1D ensures survival of apoptosis-resistant DARE cells by preventing lethal effector caspase activation, while Myo7A/Crinkled promotes effector caspase activation in the same cells. This positions Myo1D as a molecular switch controlling the threshold of caspase-driven apoptosis in a radiation-induced regenerative context. |
Drosophila genetic loss-of-function analysis in wing imaginal disc after ionizing radiation, caspase activity reporters, genetic interaction with Myo7A/Crinkled |
Nature communications |
Medium |
41345088
|
| 2022 |
miR-217-5p targets MYO1D in rat podocytes, as validated by luciferase reporter assay, qRT-PCR, and Western blotting. Myo1d is predicted to be involved in actin filament organization in podocytes, and its downregulation by miR-217-5p is associated with podocyte morphological changes including shrunken cells with abnormal actin cytoskeletons. |
Luciferase reporter assay, qRT-PCR, Western blot (miRNA-target validation) |
Non-coding RNA |
Low |
35736640
|