Musculus morbidus, una E3 ubiquitín ligasa de "drosophila", genera artrina y mantiene la integridad del sarcómero
Author
Carrasco Rando, MartaAdvisor
Ruiz Gómez, María del MarEntity
UAM. Departamento de Biología MolecularDate
2006-02-02Subjects
Drosophilas - Genética - Tesis doctorales; Biología y Biomedicina / BiologíaNote
Tesis doctoral inédita leída en la Universidad Autónoma de Madrid, Facultad de Ciencias, Departamento de Biología Molecular. Fecha de lectura: 02-02-2006Abstract
In Drosophila, as in vertebrates, the muscles are syncitia that arise through the fusion of
myoblasts.The fusion process is asymmetric and requires the prior segregation of the myogenic
mesoderm into two distinct populations of myoblasts: the founders and the fusion competent
cells. The founders have al1 the information required to give rise to a particular muscle, and
by attracting íusion competent cells to their vicinity and fusing to them they recruit them to
their specific genetic programmes. Furthermore, in mutants where fusion is blocked, founders
are the only myoblasts that complete myogenesis. Thus, these myoblasts not only carry the
particular information needed to seed individual muscles, but also must express certain genes
that enable them with the ability to initiate and execute the myogenic programme.
In an attempt to identify such genes we initiated the search of genes whose pattern of
expression was restricted to the founder population. That was the case of CC17492, that we
renamed rnusculus morbidus (murno). mumo encodes an E3 ubiquitin ligase whose function is
essential to complete myogenesis. Thus, mumo mutant embryos elaborate a wild type pattern
of muscles, indicating that neither the segregation, nor the specification of founders is altered.
However, the differentiation of the fibres is defective and is obvious both in the somatic as
well as in the visceral musculature. We show that Mumo is required for the maintenance
of Z band integrity in larval niuscles and to stabilize the attachment to the epidermis. In
addition, we show that mumo loss of function produces the same effect in the adult muscles,
where it accumulates in the Z disc. We also demonstrate that Mumo is the E3 ubiquitin ligase
responsible for the synthesis of Arthrin, a stable mono-ubiquitinated form of Actin found in the
indirect flight muscles (IFM). Again, in adult muscles Mumo is required for the maintenance of
sarcomere integrity. Our data support the idea that the failure in producing Arthrin is not the
sole responsible of the observed phenotype, suggesting that, either Mumo is acting on other
substrates or it has an additional structural function on the sarcomere.
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