4cfq

Structural highlights

Disease

[MYH9_HUMAN] MYH9-related thrombocytopenia;Autosomal dominant nonsyndromic sensorineural deafness type DFNA. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. Subjects with mutations in the motor domain of MYH9 present with severe thrombocytopenia and develop nephritis and deafness before the age of 40 years, while those with mutations in the tail domain have a much lower risk of noncongenital complications and significantly higher platelet counts. The clinical course of patients with mutations in the four most frequently affected residues of MYH9 (responsible for 70% of MYH9-related cases) were evaluated. Mutations at residue 1933 do not induce kidney damage or cataracts and cause deafness only in the elderly, those in position 702 result in severe thrombocytopenia and produce nephritis and deafness at a juvenile age, while alterations at residue 1424 or 1841 result in intermediate clinical pictures. Genetic variations in MYH9 are associated with non-diabetic end stage renal disease (ESRD).

Function

[MYH9_HUMAN] Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10.^[1]

See Also

• S100 protein

References

1. ↑ Betapudi V. Myosin II motor proteins with different functions determine the fate of lamellipodia extension during cell spreading. PLoS One. 2010 Jan 5;5(1):e8560. doi: 10.1371/journal.pone.0008560. PMID:20052411 doi:http://dx.doi.org/10.1371/journal.pone.0008560
2. ↑ Duelli A, Kiss B, Lundholm I, Bodor A, Petoukhov MV, Svergun DI, Nyitray L, Katona G. The C-Terminal Random Coil Region Tunes the Ca2+-Binding Affinity of S100A4 through Conformational Activation. PLoS One. 2014 May 15;9(5):e97654. doi: 10.1371/journal.pone.0097654. eCollection, 2014. PMID:24830809 doi:http://dx.doi.org/10.1371/journal.pone.0097654