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Role of KASH domain lengths in the regulation of LINC complexes.
Jahed, Zeinab; Hao, Hongyan; Thakkar, Vyom; Vu, Uyen T; Valdez, Venecia A; Rathish, Akshay; Tolentino, Chris; Kim, Samuel C J; Fadavi, Darya; Starr, Daniel A; Mofrad, Mohammad R K.
Afiliación
  • Jahed Z; Molecular Cell Biomechanics Laboratory, Departments of Bioengineering and Mechanical Engineering, University of California, Berkeley, Berkeley, CA 94720.
  • Hao H; Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA 95616.
  • Thakkar V; Molecular Cell Biomechanics Laboratory, Departments of Bioengineering and Mechanical Engineering, University of California, Berkeley, Berkeley, CA 94720.
  • Vu UT; Molecular Cell Biomechanics Laboratory, Departments of Bioengineering and Mechanical Engineering, University of California, Berkeley, Berkeley, CA 94720.
  • Valdez VA; Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA 95616.
  • Rathish A; Molecular Cell Biomechanics Laboratory, Departments of Bioengineering and Mechanical Engineering, University of California, Berkeley, Berkeley, CA 94720.
  • Tolentino C; Molecular Cell Biomechanics Laboratory, Departments of Bioengineering and Mechanical Engineering, University of California, Berkeley, Berkeley, CA 94720.
  • Kim SCJ; Molecular Cell Biomechanics Laboratory, Departments of Bioengineering and Mechanical Engineering, University of California, Berkeley, Berkeley, CA 94720.
  • Fadavi D; Molecular Cell Biomechanics Laboratory, Departments of Bioengineering and Mechanical Engineering, University of California, Berkeley, Berkeley, CA 94720.
  • Starr DA; Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA 95616.
  • Mofrad MRK; Molecular Cell Biomechanics Laboratory, Departments of Bioengineering and Mechanical Engineering, University of California, Berkeley, Berkeley, CA 94720.
Mol Biol Cell ; 30(16): 2076-2086, 2019 07 22.
Article en En | MEDLINE | ID: mdl-30995155
ABSTRACT
The linker of the nucleoskeleton and cytoskeleton (LINC) complex is formed by the conserved interactions between Sad-1 and UNC-84 (SUN) and Klarsicht, ANC-1, SYNE homology (KASH) domain proteins, providing a physical coupling between the nucleoskeleton and cytoskeleton that mediates the transfer of physical forces across the nuclear envelope. The LINC complex can perform distinct cellular functions by pairing various KASH domain proteins with the same SUN domain protein. For example, in Caenorhabditis elegans, SUN protein UNC-84 binds to two KASH proteins UNC-83 and ANC-1 to mediate nuclear migration and anchorage, respectively. In addition to distinct cytoplasmic domains, the luminal KASH domain also varies among KASH domain proteins of distinct functions. In this study, we combined in vivo C. elegans genetics and in silico molecular dynamics simulations to understand the relation between the length and amino acid composition of the luminal KASH domain, and the function of the SUN-KASH complex. We show that longer KASH domains can withstand and transfer higher forces and interact with the membrane through a conserved membrane proximal EEDY domain that is unique to longer KASH domains. In agreement with our models, our in vivo results show that swapping the KASH domains of ANC-1 and UNC-83, or shortening the KASH domain of ANC-1, both result in a nuclear anchorage defect in C. elegans.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Complejos Multiproteicos Límite: Animals / Humans Idioma: En Revista: Mol Biol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2019 Tipo del documento: Article
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Complejos Multiproteicos Límite: Animals / Humans Idioma: En Revista: Mol Biol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2019 Tipo del documento: Article