Matches in SemOpenAlex for { <https://semopenalex.org/work/W2914926712> ?p ?o ?g. }
Showing items 1 to 75 of
75
with 100 items per page.
- W2914926712 endingPage "412a" @default.
- W2914926712 startingPage "412a" @default.
- W2914926712 abstract "The linker of the nucleoskeleton and cytoskeleton (LINC) complexes are composed of inner nuclear membrane Sad1/UNC-84 (SUN, and outer nuclear membrane Klarsicht/ANC-1/SYNE homology (KASH) proteins. LINC complexes span the physical barrier of the nuclear envelope and regulate the physical connection between the interior of the nucleus and the cytoplasm during various cellular functions. The large cytoplasmic domains of KASH proteins bind to various elements of the cytoskeleton, whereas their 10-30 amino acid KASH domains reside in the perinuclear space (PNS) where they bind to SUN proteins. Interestingly, different KASH domain proteins can independently bind to the same SUN protein to mediate distinct cellular functions. For example, in mammals the SUN protein SUN1 can transiently associate with KASH5 in the PNS to mediate meiotic chromosome movement. Alternatively, SUN1 can bind to Nesprin1/2 to mediate nuclear movement. Similarly, in Caenorhabditis elegans (C. elegans) SUN protein UNC-84 transiently binds to KASH protein UNC-83 in embryonic hypodermal cells to mediate nuclear migration. Later, the same SUN protein UNC-84 independently binds to a different KASH protein ANC-1 to anchor of the nucleus in place for several days. In this work, we combined in vivo C. elegans genetics and in silico molecular dynamics simulations to explore the role of KASH domain length on the function of the SUN-KASH complex and its response to mechanical forces. Our results imply that longer KASH domains can withstand and transfer higher forces across the SUN-KASH complex. Additionally, our results suggest that longer KASH domains can interact with the membrane through a conserved membrane proximal EEDY domain that is unique to longer KASH domains. Finally, we 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." @default.
- W2914926712 created "2019-02-21" @default.
- W2914926712 creator A5003117798 @default.
- W2914926712 creator A5019620552 @default.
- W2914926712 creator A5038772482 @default.
- W2914926712 creator A5047221605 @default.
- W2914926712 creator A5054729232 @default.
- W2914926712 creator A5060153253 @default.
- W2914926712 creator A5062246663 @default.
- W2914926712 creator A5072156731 @default.
- W2914926712 creator A5081607337 @default.
- W2914926712 date "2019-02-01" @default.
- W2914926712 modified "2023-10-14" @default.
- W2914926712 title "Length of KASH Domains Affect Linc Complex Functions" @default.
- W2914926712 doi "https://doi.org/10.1016/j.bpj.2018.11.2223" @default.
- W2914926712 hasPublicationYear "2019" @default.
- W2914926712 type Work @default.
- W2914926712 sameAs 2914926712 @default.
- W2914926712 citedByCount "0" @default.
- W2914926712 crossrefType "journal-article" @default.
- W2914926712 hasAuthorship W2914926712A5003117798 @default.
- W2914926712 hasAuthorship W2914926712A5019620552 @default.
- W2914926712 hasAuthorship W2914926712A5038772482 @default.
- W2914926712 hasAuthorship W2914926712A5047221605 @default.
- W2914926712 hasAuthorship W2914926712A5054729232 @default.
- W2914926712 hasAuthorship W2914926712A5060153253 @default.
- W2914926712 hasAuthorship W2914926712A5062246663 @default.
- W2914926712 hasAuthorship W2914926712A5072156731 @default.
- W2914926712 hasAuthorship W2914926712A5081607337 @default.
- W2914926712 hasBestOaLocation W29149267121 @default.
- W2914926712 hasConcept C104317684 @default.
- W2914926712 hasConcept C142669718 @default.
- W2914926712 hasConcept C1491633281 @default.
- W2914926712 hasConcept C190062978 @default.
- W2914926712 hasConcept C2778944004 @default.
- W2914926712 hasConcept C28859421 @default.
- W2914926712 hasConcept C29512474 @default.
- W2914926712 hasConcept C54355233 @default.
- W2914926712 hasConcept C65871279 @default.
- W2914926712 hasConcept C86339819 @default.
- W2914926712 hasConcept C86803240 @default.
- W2914926712 hasConcept C95444343 @default.
- W2914926712 hasConceptScore W2914926712C104317684 @default.
- W2914926712 hasConceptScore W2914926712C142669718 @default.
- W2914926712 hasConceptScore W2914926712C1491633281 @default.
- W2914926712 hasConceptScore W2914926712C190062978 @default.
- W2914926712 hasConceptScore W2914926712C2778944004 @default.
- W2914926712 hasConceptScore W2914926712C28859421 @default.
- W2914926712 hasConceptScore W2914926712C29512474 @default.
- W2914926712 hasConceptScore W2914926712C54355233 @default.
- W2914926712 hasConceptScore W2914926712C65871279 @default.
- W2914926712 hasConceptScore W2914926712C86339819 @default.
- W2914926712 hasConceptScore W2914926712C86803240 @default.
- W2914926712 hasConceptScore W2914926712C95444343 @default.
- W2914926712 hasIssue "3" @default.
- W2914926712 hasLocation W29149267121 @default.
- W2914926712 hasOpenAccess W2914926712 @default.
- W2914926712 hasPrimaryLocation W29149267121 @default.
- W2914926712 hasRelatedWork W113776368 @default.
- W2914926712 hasRelatedWork W1907693897 @default.
- W2914926712 hasRelatedWork W2011649455 @default.
- W2914926712 hasRelatedWork W2031255905 @default.
- W2914926712 hasRelatedWork W2036683859 @default.
- W2914926712 hasRelatedWork W2209111398 @default.
- W2914926712 hasRelatedWork W2419291131 @default.
- W2914926712 hasRelatedWork W2772204201 @default.
- W2914926712 hasRelatedWork W3048247788 @default.
- W2914926712 hasRelatedWork W4366481708 @default.
- W2914926712 hasVolume "116" @default.
- W2914926712 isParatext "false" @default.
- W2914926712 isRetracted "false" @default.
- W2914926712 magId "2914926712" @default.
- W2914926712 workType "article" @default.