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    UNC45A unc-45 myosin chaperone A [ Homo sapiens (human) ]

    Gene ID: 55898, updated on 3-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Aagenaes syndrome/lymphedema cholestasis syndrome 1 is caused by a founder variant in the 5'-untranslated region of UNC45A.

    Aagenaes syndrome/lymphedema cholestasis syndrome 1 is caused by a founder variant in the 5'-untranslated region of UNC45A.
    Almaas R, Atneosen-Åsegg M, Ytre-Arne ME, Melheim M, Sorte HS, Cízková D, Reims HM, Bezrouk A, Harrison SP, Strand J, Hermansen JU, Andersen SS, Eiklid KL, Mokrý J, Sullivan GJ, Stray-Pedersen A.

    09/25/2023
    A Functional Relationship Between UNC45A and MYO5B Connects Two Rare Diseases With Shared Enteropathy.

    A Functional Relationship Between UNC45A and MYO5B Connects Two Rare Diseases With Shared Enteropathy.
    Li Q, Zhou Z, Sun Y, Sun C, Klappe K, van IJzendoorn SCD., Free PMC Article

    07/30/2022
    UNC45A deficiency causes microvillus inclusion disease-like phenotype by impairing myosin VB-dependent apical trafficking.

    UNC45A deficiency causes microvillus inclusion disease-like phenotype by impairing myosin VB-dependent apical trafficking.
    Duclaux-Loras R, Lebreton C, Berthelet J, Charbit-Henrion F, Nicolle O, Revenu des Courtils C, Waich S, Valovka T, Khiat A, Rabant M, Racine C, Guerrera IC, Baptista J, Mahe MM, Hess MW, Durel B, Lefort N, Banal C, Parisot M, Talbotec C, Lacaille F, Ecochard-Dugelay E, Demir AM, Vogel GF, Faivre L, Rodrigues A, Fowler D, Janecke AR, Müller T, Huber LA, Rodrigues-Lima F, Ruemmele FM, Uhlig HH, Del Bene F, Michaux G, Cerf-Bensussan N, Parlato M., Free PMC Article

    05/21/2022
    A myosin chaperone, UNC-45A, is a novel regulator of intestinal epithelial barrier integrity and repair.

    A myosin chaperone, UNC-45A, is a novel regulator of intestinal epithelial barrier integrity and repair.
    Lechuga S, Cartagena-Rivera AX, Khan A, Crawford BI, Narayanan V, Conway DE, Lehtimäki J, Lappalainen P, Rieder F, Longworth MS, Ivanov AI., Free PMC Article

    04/23/2022
    UNC-45A breaks the microtubule lattice independently of its effects on non-muscle myosin II.

    UNC-45A breaks the microtubule lattice independently of its effects on non-muscle myosin II.
    Habicht J, Mooneyham A, Hoshino A, Shetty M, Zhang X, Emmings E, Yang Q, Coombes C, Gardner MK, Bazzaro M., Free PMC Article

    08/7/2021
    In cells, UNC-45A binds to and destabilizes mitotic spindles, and its depletion causes severe defects in chromosome congression and segregation. UNC-45A is overexpressed in human clinical specimens from chemoresistant ovarian cancer and that UNC-45A-overexpressing cells resist chromosome missegregation and aneuploidy when treated with clinically relevant concentrations of paclitaxel.

    UNC-45A Is a Novel Microtubule-Associated Protein and Regulator of Paclitaxel Sensitivity in Ovarian Cancer Cells.
    Mooneyham A, Iizuka Y, Yang Q, Coombes C, McClellan M, Shridhar V, Emmings E, Shetty M, Chen L, Ai T, Meints J, Lee MK, Gardner M, Bazzaro M., Free PMC Article

    02/1/2020
    The co-chaperone UNC45A is essential for the expression of mitotic kinase NEK7 and tumorigenesis.

    The co-chaperone UNC45A is essential for the expression of mitotic kinase NEK7 and tumorigenesis.
    Eisa NH, Jilani Y, Kainth K, Redd P, Lu S, Bougrine O, Abdul Sater H, Patwardhan CA, Shull A, Shi H, Liu K, Elsherbiny NM, Eissa LA, El-Shishtawy MM, Horuzsko A, Bollag R, Maihle N, Roig J, Korkaya H, Cowell JK, Chadli A., Free PMC Article

    10/19/2019
    A transient induction of the human UNC45-GC, but not UNC45-SM, could rescue the defective endocytosis in these she4Delta cells at 39 degrees C, irrespective of whether they possessed Hsp90alpha or Hsp90beta.

    UCS protein function is partially restored in the Saccharomyces cerevisiae she4 mutant with expression of the human UNC45-GC, but not UNC45-SM.
    Escalante SG, Brightmore JA, Piper PW, Millson SH., Free PMC Article

    01/26/2019
    Whole-exome sequencing of all affected individuals and their parents identified biallelic mutations in Unc-45 Myosin Chaperone A (UNC45A) as a likely driver for cholestasis, congenital diarrhea, impaired hearing, and bone fragility.

    Loss-of-Function Mutations in UNC45A Cause a Syndrome Associating Cholestasis, Diarrhea, Impaired Hearing, and Bone Fragility.
    Esteve C, Francescatto L, Tan PL, Bourchany A, De Leusse C, Marinier E, Blanchard A, Bourgeois P, Brochier-Armanet C, Bruel AL, Delarue A, Duffourd Y, Ecochard-Dugelay E, Hery G, Huet F, Gauchez P, Gonzales E, Guettier-Bouttier C, Komuta M, Lacoste C, Maudinas R, Mazodier K, Rimet Y, Rivière JB, Roquelaure B, Sigaudy S, Stephenne X, Thauvin-Robinet C, Thevenon J, Sarles J, Levy N, Badens C, Goulet O, Hugot JP, Katsanis N, Faivre L, Fabre A., Free PMC Article

    12/22/2018
    UNC-45a promotes generation of contractile actomyosin bundles through synchronized non-muscle myosin II folding and filament-assembly activities.

    UNC-45a promotes myosin folding and stress fiber assembly.
    Lehtimäki JI, Fenix AM, Kotila TM, Balistreri G, Paavolainen L, Varjosalo M, Burnette DT, Lappalainen P., Free PMC Article

    12/9/2017
    Results provide novel insights into the molecular mechanisms of neurite growth and define UNC-45A as a novel and master regulator of NMII-mediated cellular processes in neurons.

    UNC-45A is required for neurite extension via controlling NMII activation.
    Iizuka Y, Mooneyham A, Sieben A, Chen K, Maile M, Hellweg R, Schütz F, Teckle K, Starr T, Thayanithy V, Vogel RI, Lou E, Lee MK, Bazzaro M., Free PMC Article

    10/7/2017
    UNC-45A is a crucial component in regulating human NK cell cytoskeletal dynamics via promoting the formation of actomyosin complexes.

    UNC-45A Is a Nonmuscle Myosin IIA Chaperone Required for NK Cell Cytotoxicity via Control of Lytic Granule Secretion.
    Iizuka Y, Cichocki F, Sieben A, Sforza F, Karim R, Coughlin K, Isaksson Vogel R, Gavioli R, McCullar V, Lenvik T, Lee M, Miller J, Bazzaro M., Free PMC Article

    02/27/2016
    Findings identify a novel centrosomal function for UNC45A and its role in cell proliferation and tumorigenesis.

    UNC45A localizes to centrosomes and regulates cancer cell proliferation through ChK1 activation.
    Jilani Y, Lu S, Lei H, Karnitz LM, Chadli A., Free PMC Article

    04/25/2015
    The authors found that UNC-45A is alternatively expressed at the mRNA and protein levels as two isoforms and that the two isoforms differ only by a proline-rich 15-amino-acid sequence near the amino-terminus.

    Differential turnover of myosin chaperone UNC-45A isoforms increases in metastatic human breast cancer.
    Guo W, Chen D, Fan Z, Epstein HF.

    10/29/2011
    GCUNC45 is required for the normal cellular distribution of Hsp90beta, but not Hsp90alpha.

    GCUNC45 is the first Hsp90 co-chaperone to show alpha/beta isoform specificity.
    Chadli A, Felts SJ, Toft DO., Free PMC Article

    01/21/2010
    elevated GC UNC-45 protein expression in ovarian carcinoma proliferation and metastasis.

    Myosin II co-chaperone general cell UNC-45 overexpression is associated with ovarian cancer, rapid proliferation, and motility.
    Bazzaro M, Santillan A, Lin Z, Tang T, Lee MK, Bristow RE, Shih IeM, Roden RB., Free PMC Article

    01/21/2010
    GCUNC-45 is a novel modulator of progesterone receptor chaperoning by hsp90.

    GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.
    Chadli A, Graham JD, Abel MG, Jackson TA, Gordon DF, Wood WM, Felts SJ, Horwitz KB, Toft D., Free PMC Article

    01/21/2010
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