Management of cytoskeleton architecture by molecular chaperones and immunophilins
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...
Guardado en:
| Autor principal: | |
|---|---|
| Publicado: |
2011
|
| Materias: | |
| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08986568_v23_n12_p1907_Quinta http://hdl.handle.net/20.500.12110/paper_08986568_v23_n12_p1907_Quinta |
| Aporte de: |
| id |
paper:paper_08986568_v23_n12_p1907_Quinta |
|---|---|
| record_format |
dspace |
| spelling |
paper:paper_08986568_v23_n12_p1907_Quinta2023-06-08T15:49:26Z Management of cytoskeleton architecture by molecular chaperones and immunophilins Lagadari, Mariana Folding Heat-shock protein Intermediate filament Microfilament Microtubule Stress actin apoptotic protease activating factor 1 benzyloxycarbonylleucylleucylleucinal chaperone chaperonin colchicine fk 506 binding protein fk 506 binding protein 51 fk 506 binding protein 52 gamma tubulin glial fibrillary acidic protein heat shock protein 100 heat shock protein 25 heat shock protein 27 heat shock protein 40 heat shock protein 60 heat shock protein 70 heat shock protein 90 immunophilin isothiocyanic acid derivative paclitaxel protein p23 resveratrol survivin tanespimycin tau protein tubulin unclassified drug unindexed drug vimentin vincristine antineoplastic activity cell communication cell cycle cell division cell growth cell maturation cell motion cell organelle cell vacuole complex formation cytoskeleton drug potentiation drug protein binding drug resistance heat stress human intermediate filament microtubule nerve cell differentiation nonhuman priority journal protein aggregation protein assembly protein expression protein folding protein function protein localization protein processing review Animals Cell Differentiation Cytoskeleton Glycoproteins Humans Immunophilins Inhibitor of Apoptosis Proteins Molecular Chaperones Multiprotein Complexes Neurons Protein Binding Protein Multimerization Protein Processing, Post-Translational Protein Structure, Tertiary tau Proteins 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. Fil:Lagadari, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2011 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08986568_v23_n12_p1907_Quinta http://hdl.handle.net/20.500.12110/paper_08986568_v23_n12_p1907_Quinta |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Folding Heat-shock protein Intermediate filament Microfilament Microtubule Stress actin apoptotic protease activating factor 1 benzyloxycarbonylleucylleucylleucinal chaperone chaperonin colchicine fk 506 binding protein fk 506 binding protein 51 fk 506 binding protein 52 gamma tubulin glial fibrillary acidic protein heat shock protein 100 heat shock protein 25 heat shock protein 27 heat shock protein 40 heat shock protein 60 heat shock protein 70 heat shock protein 90 immunophilin isothiocyanic acid derivative paclitaxel protein p23 resveratrol survivin tanespimycin tau protein tubulin unclassified drug unindexed drug vimentin vincristine antineoplastic activity cell communication cell cycle cell division cell growth cell maturation cell motion cell organelle cell vacuole complex formation cytoskeleton drug potentiation drug protein binding drug resistance heat stress human intermediate filament microtubule nerve cell differentiation nonhuman priority journal protein aggregation protein assembly protein expression protein folding protein function protein localization protein processing review Animals Cell Differentiation Cytoskeleton Glycoproteins Humans Immunophilins Inhibitor of Apoptosis Proteins Molecular Chaperones Multiprotein Complexes Neurons Protein Binding Protein Multimerization Protein Processing, Post-Translational Protein Structure, Tertiary tau Proteins |
| spellingShingle |
Folding Heat-shock protein Intermediate filament Microfilament Microtubule Stress actin apoptotic protease activating factor 1 benzyloxycarbonylleucylleucylleucinal chaperone chaperonin colchicine fk 506 binding protein fk 506 binding protein 51 fk 506 binding protein 52 gamma tubulin glial fibrillary acidic protein heat shock protein 100 heat shock protein 25 heat shock protein 27 heat shock protein 40 heat shock protein 60 heat shock protein 70 heat shock protein 90 immunophilin isothiocyanic acid derivative paclitaxel protein p23 resveratrol survivin tanespimycin tau protein tubulin unclassified drug unindexed drug vimentin vincristine antineoplastic activity cell communication cell cycle cell division cell growth cell maturation cell motion cell organelle cell vacuole complex formation cytoskeleton drug potentiation drug protein binding drug resistance heat stress human intermediate filament microtubule nerve cell differentiation nonhuman priority journal protein aggregation protein assembly protein expression protein folding protein function protein localization protein processing review Animals Cell Differentiation Cytoskeleton Glycoproteins Humans Immunophilins Inhibitor of Apoptosis Proteins Molecular Chaperones Multiprotein Complexes Neurons Protein Binding Protein Multimerization Protein Processing, Post-Translational Protein Structure, Tertiary tau Proteins Lagadari, Mariana Management of cytoskeleton architecture by molecular chaperones and immunophilins |
| topic_facet |
Folding Heat-shock protein Intermediate filament Microfilament Microtubule Stress actin apoptotic protease activating factor 1 benzyloxycarbonylleucylleucylleucinal chaperone chaperonin colchicine fk 506 binding protein fk 506 binding protein 51 fk 506 binding protein 52 gamma tubulin glial fibrillary acidic protein heat shock protein 100 heat shock protein 25 heat shock protein 27 heat shock protein 40 heat shock protein 60 heat shock protein 70 heat shock protein 90 immunophilin isothiocyanic acid derivative paclitaxel protein p23 resveratrol survivin tanespimycin tau protein tubulin unclassified drug unindexed drug vimentin vincristine antineoplastic activity cell communication cell cycle cell division cell growth cell maturation cell motion cell organelle cell vacuole complex formation cytoskeleton drug potentiation drug protein binding drug resistance heat stress human intermediate filament microtubule nerve cell differentiation nonhuman priority journal protein aggregation protein assembly protein expression protein folding protein function protein localization protein processing review Animals Cell Differentiation Cytoskeleton Glycoproteins Humans Immunophilins Inhibitor of Apoptosis Proteins Molecular Chaperones Multiprotein Complexes Neurons Protein Binding Protein Multimerization Protein Processing, Post-Translational Protein Structure, Tertiary tau Proteins |
| description |
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. |
| author |
Lagadari, Mariana |
| author_facet |
Lagadari, Mariana |
| author_sort |
Lagadari, Mariana |
| title |
Management of cytoskeleton architecture by molecular chaperones and immunophilins |
| title_short |
Management of cytoskeleton architecture by molecular chaperones and immunophilins |
| title_full |
Management of cytoskeleton architecture by molecular chaperones and immunophilins |
| title_fullStr |
Management of cytoskeleton architecture by molecular chaperones and immunophilins |
| title_full_unstemmed |
Management of cytoskeleton architecture by molecular chaperones and immunophilins |
| title_sort |
management of cytoskeleton architecture by molecular chaperones and immunophilins |
| publishDate |
2011 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08986568_v23_n12_p1907_Quinta http://hdl.handle.net/20.500.12110/paper_08986568_v23_n12_p1907_Quinta |
| work_keys_str_mv |
AT lagadarimariana managementofcytoskeletonarchitecturebymolecularchaperonesandimmunophilins |
| _version_ |
1768541710305984512 |