Management of cytoskeleton architecture by molecular chaperones and immunophilins

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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 transpo...

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Autor principal: Quintá, H.R
Otros Autores: Galigniana, N.M, Erlejman, A.G, Lagadari, M., Piwien-Pilipuk, G., Galigniana, M.D
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2011
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mg 132
Acceso en línea:Registro en Scopus
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Biblioteca Central Dr. Luis F. Leloir (FCEN) de Universidad de Buenos Aires
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024 7 |2 scopus  |a 2-s2.0-80053269920 
024 7 |2 cas  |a apoptotic protease activating factor 1, 215953-91-6; benzyloxycarbonylleucylleucylleucinal, 133407-82-6; colchicine, 64-86-8; gamma tubulin, 138757-07-0; paclitaxel, 33069-62-4; resveratrol, 501-36-0; survivin, 195263-98-0; tanespimycin, 75747-14-7; vincristine, 57-22-7; Glycoproteins; Immunophilins, 5.2.1.8; Inhibitor of Apoptosis Proteins; Molecular Chaperones; Multiprotein Complexes; tau Proteins; tissue-factor-pathway inhibitor 2 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a CESIE 
100 1 |a Quintá, H.R. 
245 1 0 |a Management of cytoskeleton architecture by molecular chaperones and immunophilins 
260 |c 2011 
270 1 0 |m Galigniana, M.D.; Inst. de Biologia y Medicina Experimental, CONICET, Vuelta de Obligado 2490, Buenos Aires (C1428ADN), Argentina; email: mgali@qb.fcen.uba.ar 
506 |2 openaire  |e Política editorial 
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520 3 |a 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 only 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 of 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 tumor 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. © 2011 Elsevier Inc.  |l eng 
536 |a Detalles de la financiación: Daniel and Florence Guggenheim Foundation, PICT 2007–0640 
536 |a Detalles de la financiación: Universidad de Buenos Aires 
536 |a Detalles de la financiación: National Institutes of Health, R03TW008143-01A1 
536 |a Detalles de la financiación: Agencia Nacional de Promoción Científica y Tecnológica, PICT 2010–1170 
536 |a Detalles de la financiación: The experimental work described in this review was supported by grants from Universidad de Buenos Aires (UBACyT Program). ANPCyT PICT 2010–1170 and the Guggenheim Foundation (to M.D.G.), and ANPCyT PICT 2007–0640 and NIH -FIRCA award R03TW008143-01A1 (to G.P.P.). 
593 |a Instituto de Biologia y Medicina Experimental-CONICET, Vuelta de Obligado 2490, Buenos Aires (C1428ADN), Argentina 
593 |a Departamento de Quimica Biologica, Facultad de Ciencias Exactas y Naturales, Univ. de Buenos Aires, Ciudad Universitaria, Buenos Aires (C1428EGA), Argentina 
690 1 0 |a FOLDING 
690 1 0 |a HEAT-SHOCK PROTEIN 
690 1 0 |a INTERMEDIATE FILAMENT 
690 1 0 |a MICROFILAMENT 
690 1 0 |a MICROTUBULE 
690 1 0 |a STRESS 
690 1 0 |a ACTIN 
690 1 0 |a APOPTOTIC PROTEASE ACTIVATING FACTOR 1 
690 1 0 |a BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL 
690 1 0 |a CHAPERONE 
690 1 0 |a CHAPERONIN 
690 1 0 |a COLCHICINE 
690 1 0 |a FK 506 BINDING PROTEIN 
690 1 0 |a FK 506 BINDING PROTEIN 51 
690 1 0 |a FK 506 BINDING PROTEIN 52 
690 1 0 |a GAMMA TUBULIN 
690 1 0 |a GLIAL FIBRILLARY ACIDIC PROTEIN 
690 1 0 |a HEAT SHOCK PROTEIN 100 
690 1 0 |a HEAT SHOCK PROTEIN 25 
690 1 0 |a HEAT SHOCK PROTEIN 27 
690 1 0 |a HEAT SHOCK PROTEIN 40 
690 1 0 |a HEAT SHOCK PROTEIN 60 
690 1 0 |a HEAT SHOCK PROTEIN 70 
690 1 0 |a HEAT SHOCK PROTEIN 90 
690 1 0 |a IMMUNOPHILIN 
690 1 0 |a ISOTHIOCYANIC ACID DERIVATIVE 
690 1 0 |a PACLITAXEL 
690 1 0 |a PROTEIN P23 
690 1 0 |a RESVERATROL 
690 1 0 |a SURVIVIN 
690 1 0 |a TANESPIMYCIN 
690 1 0 |a TAU PROTEIN 
690 1 0 |a TUBULIN 
690 1 0 |a UNCLASSIFIED DRUG 
690 1 0 |a UNINDEXED DRUG 
690 1 0 |a VIMENTIN 
690 1 0 |a VINCRISTINE 
690 1 0 |a ANTINEOPLASTIC ACTIVITY 
690 1 0 |a CELL COMMUNICATION 
690 1 0 |a CELL CYCLE 
690 1 0 |a CELL DIVISION 
690 1 0 |a CELL GROWTH 
690 1 0 |a CELL MATURATION 
690 1 0 |a CELL MOTION 
690 1 0 |a CELL ORGANELLE 
690 1 0 |a CELL VACUOLE 
690 1 0 |a COMPLEX FORMATION 
690 1 0 |a CYTOSKELETON 
690 1 0 |a DRUG POTENTIATION 
690 1 0 |a DRUG PROTEIN BINDING 
690 1 0 |a DRUG RESISTANCE 
690 1 0 |a HEAT STRESS 
690 1 0 |a HUMAN 
690 1 0 |a INTERMEDIATE FILAMENT 
690 1 0 |a MICROTUBULE 
690 1 0 |a NERVE CELL DIFFERENTIATION 
690 1 0 |a NONHUMAN 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a PROTEIN AGGREGATION 
690 1 0 |a PROTEIN ASSEMBLY 
690 1 0 |a PROTEIN EXPRESSION 
690 1 0 |a PROTEIN FOLDING 
690 1 0 |a PROTEIN FUNCTION 
690 1 0 |a PROTEIN LOCALIZATION 
690 1 0 |a PROTEIN PROCESSING 
690 1 0 |a REVIEW 
690 1 0 |a ANIMALS 
690 1 0 |a CELL DIFFERENTIATION 
690 1 0 |a CYTOSKELETON 
690 1 0 |a GLYCOPROTEINS 
690 1 0 |a HUMANS 
690 1 0 |a IMMUNOPHILINS 
690 1 0 |a INHIBITOR OF APOPTOSIS PROTEINS 
690 1 0 |a MOLECULAR CHAPERONES 
690 1 0 |a MULTIPROTEIN COMPLEXES 
690 1 0 |a NEURONS 
690 1 0 |a PROTEIN BINDING 
690 1 0 |a PROTEIN MULTIMERIZATION 
690 1 0 |a PROTEIN PROCESSING, POST-TRANSLATIONAL 
690 1 0 |a PROTEIN STRUCTURE, TERTIARY 
690 1 0 |a TAU PROTEINS 
653 0 0 |a mg 132 
700 1 |a Galigniana, N.M. 
700 1 |a Erlejman, A.G. 
700 1 |a Lagadari, M. 
700 1 |a Piwien-Pilipuk, G. 
700 1 |a Galigniana, M.D. 
773 0 |d 2011  |g v. 23  |h pp. 1907-1920  |k n. 12  |p Cell. Signal.  |x 08986568  |w (AR-BaUEN)CENRE-4136  |t Cellular Signalling 
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856 4 0 |u https://doi.org/10.1016/j.cellsig.2011.07.023  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_08986568_v23_n12_p1907_Quinta  |y Handle 
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