Journal
TRENDS IN CELL BIOLOGY
Volume 18, Issue 1, Pages 28-37Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tcb.2007.11.004
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Funding
- NATIONAL CANCER INSTITUTE [R01CA122151] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES [R01AR041836, R01AR043380] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF DENTAL &CRANIOFACIAL RESEARCH [P01DE012328] Funding Source: NIH RePORTER
- NCI NIH HHS [R01CA122151] Funding Source: Medline
- NIAMS NIH HHS [R01AR41836, R01AR43380] Funding Source: Medline
- NIDCR NIH HHS [P01DE12328] Funding Source: Medline
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Intermediate filament (IF) proteins belong to a large and diverse gene family with broad representation in vertebrate tissues. Although considered the 'toughest' cytoskeletal fibers, studies in cultured cells have revealed that IF can be surprisingly dynamic and highly regulated. This review examines the diversity of IF assembly behaviors, and considers the ideas that IF proteins are co- or post-translationally assembled into oligomeric precursors, which can be delivered to different subcellular compartments by microtubulles or actomyosin and associated motor proteins. Their interaction with other cellular elements via IF associated proteins (IFAPs) affects IF dynamics and also results in cellular networks with properties that transcend those of individual components. We end by discussing how mutations leading to defects in IF assembly, network formation or IF-IFAP association compromise in vivo functions of IF as protectors against environmental stress.
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