Myosin-10 (MYH10)
The protein contains 1976 amino acids for an estimated molecular weight of 228999 Da.
Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the central part but not the margins of spreading cells), and lamellipodial extension; this function is mechanically antagonized by MYH9. (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology.
(right-click above to access to more options from the contextual menu)
| Variant | Description |
|---|---|
| Probable disease-associated variant found in a patient with severe int |
Biological Process
Actin filament-based movement
Actomyosin structure organization
Adult heart development
Aorta development
Axon guidance
Cardiac myofibril assembly
Cardiac septum development
Cell adhesion
Cell population proliferation
Cerebellar Purkinje cell layer development
Coronary vasculature development
Ephrin receptor signaling pathway
Exocytosis
Fourth ventricle development
In utero embryonic development
Lateral ventricle development
Metabolic process
Microtubule-based movement
Mitotic cytokinesis
Modification of postsynaptic actin cytoskeleton
Neuromuscular process controlling balance
Neuron migration
Nuclear migration
Plasma membrane repair
Positive regulation of protein secretion
Postsynaptic actin cytoskeleton organization
Regulation of cell shape
Retina development in camera-type eye
Substrate-dependent cell migration, cell extension
Third ventricle development
Ventricular cardiac muscle cell development
Cellular Component
Actin cytoskeleton
Actomyosin
Axon
Brush border
Cell cortex
Cleavage furrow
Cytoplasm
Cytoplasmic side of plasma membrane
Cytosol
Dendritic spine
Extracellular exosome
Glutamatergic synapse
Growth cone
Lamellipodium
Midbody
Mitochondrion
Myosin complex
Myosin II complex
Myosin II filament
Neuromuscular junction
Neuronal cell body
Nucleus
Plasma membrane
Polysome
Spindle
Stress fiber
The reference OMIM entry for this protein is 160776
Myosin, heavy chain 10, nonmuscle; myh10
Cellular myosin heavy chain, type b
Myosin, heavy chain, nonmuscle, type b; nmmhcb
Nonmuscle myosin iib
Nmhc iib
CLONING
Simons et al. (1991) cloned cDNAs encoding 2 different human nonmuscle myosin heavy chains, which they designated NMMHCA (MYH9; 160775) and NMMHCB. Both mRNAs were 7.5 kb long. By Northern blot analysis, D'Apolito et al. (2002) found that Myh10 was abundantly expressed in mouse brain and testis. It was also expressed in heart, lung, liver, and kidney, but not in skeletal muscle or spleen.GENE FUNCTION
Completion of cell division during cytokinesis requires temporally and spatially regulated communication from the microtubule cytoskeleton to the actin cytoskeleton and the cell membrane. Straight et al. (2003) identified a specific inhibitor of nonmuscle myosin II, blebbistatin, that inhibited contraction of the cleavage furrow without disrupting mitosis or contractile ring assembly. Using blebbistatin and other drugs, Straight et al. (2003) showed that exit from the cytokinetic phase of the cell cycle depends on ubiquitin-mediated proteolysis. Continuous signals from microtubules are required to maintain the position of the cleavage furrow, and these signals control the localization of myosin II independently of other furrow components. Turney and Bridgman (2005) found that Myh10 was required by embryonic rat peripheral nerve growth cones to turn at borders of laminin (see LAMA2; 156225) stripes in response to signals from laminin-activated integrin receptors. In the absence of Myh10, neurite outgrowth continued across laminin borders. Kim et al. (2005) found that actin-activated MgATPase activity was decreased in MYH10 with either an asn97-to-lysine (N97K) substitution, which is homologous to the N93K mutation in MYH9 (160775.0003) that causes May-Hegglin anomaly (155100), or an arg709-to-cysteine (R709C) substitution, which causes developmental defects in brain and heart when present in mouse Myh10. The ability of MYH10 heavy meromyosin to support the movement of actin filaments over an MYH10-coated surface was reduced in heavy meromyosin with the N97K mutation and eliminated with the R709C mutation. Kinetic analysis indicated that the R709C mutation resulted in extremely tight affinity between MYH10 heavy meromyosin and ADP, reducing the rate of ADP release. Ryu et al. (2006) showed that Myh10 was enriched in the postsynaptic density of rat hippocampal neurons and was essential for normal spine morphology and dynamics. Pharmacologic or genetic inhibition of Myh10 altered protrusive motility of spines, destabilized their mushroom-head morphology, and impaired excitatory synaptic transmission. Using immunofluorescence microscopy, Western blot analysis, and knockdown strategies with human lung fibroblasts, Hanisch et al. (2011) showed that Salmonella entered nonphagocytic cells by manipulating 2 machineries of actin-based motility in the host: actin polymerization through the ARP2/3 complex (604221), and actomyosin-mediated contractility in a myosin IIA- and myosin IIB-dependent manner. Hanisch et al. (2011) concluded that Salmonella entry can be effected independently of membrane ruffling.MAPPING
By study of hybrid panels and by in situ hybridization, Simons et al. (1991) localized the MYH10 gene to chromosome 17p13. The assignment is shared by several other skeletal muscle heavy chain genes.MOLECULAR GENETICS
For discussion of a possible association between variation in the MYH10 gene and a complex neurologic phenotype, see 160776.0001 and 160776.0002.ANIMAL MODEL
Taked ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 160776 was added.