INVESTIGADORES
ERLEJMAN Alejandra Giselle
artículos
Título:
Management of cytoskeleton architecture by molecular chaperones and Immunophilins
Autor/es:
QUINTÁ E.R.; GALIGNIANA N.M.; ERLEJMAN A.G.; LAGADARI M.; PIWIEN PILIPUK G.; GALIGNIANA M.D.
Revista:
CELLULAR SIGNALLING
Editorial:
ELSEVIER SCIENCE INC
Referencias:
Lugar: Amsterdam; Año: 2011 vol. 23 p. 1907 - 1920
ISSN:
0898-6568
Resumen:
Cytoskeletal structure is continually remodeled to accommodate normal cell growth and to
respond to pathophysiological cues. As a consequence, several cytoskeleton-interacting proteins
become involved in a variety of cellular processes such as cell growth and division, cell movement,
vesicle transportation, cellular organelle location and function, localization and distribution of
membrane receptors, and cell-cell communication. Molecular chaperones and immunophilins are
counted among the most important proteins that interact closely with the cytoskeleton network, in
particular with microtubules and microtubule-associated factors. In several situations, heat-shock
proteins and immunophilins work together as a functionally active heterocomplex, although both
types of proteins also show independent actions. In circumstances where homeostasis is affected by
environmental stresses or due to genetic alterations, chaperone proteins help to stabilize the system.
Molecular chaperones facilitate the assembly, disassembly and/or folding/refolding of cytoskeletal
proteins, so they prevent aberrant protein aggregation. Nonetheless, the roles of heat-shock proteins
and immunophilins are not limited to solve abnormal situations, but they also have an active
participation during the normal differentiation process of the cell and are key factors for many
structural and functional rearrangements during this course of action. Cytoskeleton modifications
leading to altered localization nuclear factors may result in loss- or gain-of-function of such factors,
which affects the cell cycle and cell development. Therefore, cytoskeletal components are attractive
therapeutic targets, particularly microtubules, to prevent pathological situations such as rapidly
dividing tumour cells or to favor the process of cell differentiation in other cases. In this review we
will address some classical and novel aspects of key regulatory functions of heat-shock proteins and
immunophilins as housekeeping factors of the cytoskeletal network.