Please use this identifier to cite or link to this item: https://doi.org/10.21256/zhaw-22109
Full metadata record
DC FieldValueLanguage
dc.contributor.authorKozono, Takuma-
dc.contributor.authorSato, Hiroyuki-
dc.contributor.authorOkumura, Wataru-
dc.contributor.authorJogano, Chifuyu-
dc.contributor.authorTamura-Nakano, Miwa-
dc.contributor.authorKawamura, Yuki I.-
dc.contributor.authorRohrer, Jack-
dc.contributor.authorTonozuka, Takashi-
dc.contributor.authorNishikawa, Atsushi-
dc.date.accessioned2021-03-15T14:52:30Z-
dc.date.available2021-03-15T14:52:30Z-
dc.date.issued2021-
dc.identifier.issn2045-2322de_CH
dc.identifier.urihttps://digitalcollection.zhaw.ch/handle/11475/22109-
dc.description.abstractJaw1/LRMP is a type II integral membrane protein that is localized at the endoplasmic reticulum (ER) and outer nuclear membrane. We previously reported that a function of Jaw1 is to maintain the nuclear shape as a KASH protein via its carboxyl terminal region, a component of linker of nucleoskeleton and cytoskeleton complex in the oligomeric state. Although the oligomerization of some KASH proteins via the cytosolic regions serves to stabilize protein-protein interactions, the issue of how the oligomerization of Jaw1 is regulated is not completely understood. Therefore, we focused on three distinct regions on the cytosolic face of Jaw1: the N-terminal region, the coiled-coil domain and the stem region, in terms of oligomerization. A co-immunoprecipitation assay showed that its coiled-coil domain is a candidate for the oligomerization site. Furthermore, our data indicated that the N-terminal region prevents the aberrant oligomerization of Jaw1 as an intrinsically disordered region (IDR). Importantly, the ectopic expression of an N-terminal region deleted mutant caused the formation of organized smooth ER (OSER), structures such as nuclear karmellae and whorls, in B16F10 cells. Furthermore, this OSER interfered with the localization of the oligomer and interactors such as the type III inositol 1,4,5-triphosphate receptor (IP3R3) and SUN2. In summary, the N-terminal region of Jaw1 inhibits the formation of OSER as an IDR to maintain the homeostatic localization of interactors on the ER membrane.de_CH
dc.language.isoende_CH
dc.publisherNature Publishing Groupde_CH
dc.relation.ispartofScientific Reportsde_CH
dc.rightshttp://creativecommons.org/licenses/by/4.0/de_CH
dc.subjectOrganellesde_CH
dc.subjectMembrane structure and assemblyde_CH
dc.subjectIntrinsically disordered proteinde_CH
dc.subject.ddc572: Biochemiede_CH
dc.titleThe N-terminal region of Jaw1 has a role to inhibit the formation of organized smooth endoplasmic reticulum as an intrinsically disordered regionde_CH
dc.typeBeitrag in wissenschaftlicher Zeitschriftde_CH
dcterms.typeTextde_CH
zhaw.departementLife Sciences und Facility Managementde_CH
zhaw.organisationalunitInstitut für Chemie und Biotechnologie (ICBT)de_CH
dc.identifier.doi10.1038/s41598-020-80258-5de_CH
dc.identifier.doi10.21256/zhaw-22109-
dc.identifier.pmid33436890de_CH
zhaw.funding.euNode_CH
zhaw.issue753de_CH
zhaw.originated.zhawYesde_CH
zhaw.publication.statuspublishedVersionde_CH
zhaw.volume11de_CH
zhaw.publication.reviewPeer review (Publikation)de_CH
zhaw.webfeedZellphysiologiede_CH
zhaw.author.additionalNode_CH
zhaw.display.portraitYesde_CH
Appears in collections:Publikationen Life Sciences und Facility Management

Files in This Item:
File Description SizeFormat 
2021_Kozono-etal_N-terminal-region-of-Jaw1.pdf8.18 MBAdobe PDFThumbnail
View/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.