Non-muscle myosin heavy chain IIA and IIB interact and co-localize in living cells: Relevance for MYH9-related disease

  • Authors:
    • Monica Marini
    • Maurizio Bruschi
    • Alessandro Pecci
    • Roberta Romagnoli
    • Luca Musante
    • Giovanni Candiano
    • Gian Marco Ghiggeri
    • Carlo Balduini
    • Marco Seri
    • Roberto Ravazzolo
  • View Affiliations

  • Published online on: May 1, 2006     https://doi.org/10.3892/ijmm.17.5.729
  • Pages: 729-736
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Abstract

Myosins of class II constitute part of a superfamily of several classes of proteins expressed in almost all eukaryotic cell types. Differences in the heavy chains produce three isoforms of class II non-muscle myosins (A, B and C), which are widely distributed in most tissues and thought to be components of the cell motor systems, although specific functional roles are largely unknown. In particular, it is still a matter of debate whether they interact and have overlapping or distinct functions. This argument is relevant not only to cell physiology, but also to human pathology since mutations of the MYH9 gene encoding non-muscle myosin heavy chain II A (NMMHC-A) cause MYH9-related disease (MYH9-RD), an autosomal dominant disorder characterized by platelet macrocytosis, thrombocytopenia and leukocyte inclusions, variably associated with sensorineural hearing loss, cataracts and/or glomerulonephritis. In this study, we report the results of yeast two-hybrid screening showing that the C-terminals of NMMHC-A and -B interact. This interaction was confirmed by immunoprecipitation in transfected COS-7 cells and in skin fibroblasts naturally expressing both isoforms. Moreover, our immunomorphological study revealed that isoforms A and B co-localize in fibroblasts, erythroblasts and kidney cells. These results suggest that isoforms A and B are strictly related molecules and support the hypothesis that their interrelationship could be involved both in the variability of clinical phenotype and selectivity of tissue damage of MYH9-RD.

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May 2006
Volume 17 Issue 5

Print ISSN: 1107-3756
Online ISSN:1791-244X

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Spandidos Publications style
Marini M, Bruschi M, Pecci A, Romagnoli R, Musante L, Candiano G, Ghiggeri GM, Balduini C, Seri M, Ravazzolo R, Ravazzolo R, et al: Non-muscle myosin heavy chain IIA and IIB interact and co-localize in living cells: Relevance for MYH9-related disease. Int J Mol Med 17: 729-736, 2006
APA
Marini, M., Bruschi, M., Pecci, A., Romagnoli, R., Musante, L., Candiano, G. ... Ravazzolo, R. (2006). Non-muscle myosin heavy chain IIA and IIB interact and co-localize in living cells: Relevance for MYH9-related disease. International Journal of Molecular Medicine, 17, 729-736. https://doi.org/10.3892/ijmm.17.5.729
MLA
Marini, M., Bruschi, M., Pecci, A., Romagnoli, R., Musante, L., Candiano, G., Ghiggeri, G. M., Balduini, C., Seri, M., Ravazzolo, R."Non-muscle myosin heavy chain IIA and IIB interact and co-localize in living cells: Relevance for MYH9-related disease". International Journal of Molecular Medicine 17.5 (2006): 729-736.
Chicago
Marini, M., Bruschi, M., Pecci, A., Romagnoli, R., Musante, L., Candiano, G., Ghiggeri, G. M., Balduini, C., Seri, M., Ravazzolo, R."Non-muscle myosin heavy chain IIA and IIB interact and co-localize in living cells: Relevance for MYH9-related disease". International Journal of Molecular Medicine 17, no. 5 (2006): 729-736. https://doi.org/10.3892/ijmm.17.5.729