Please use this identifier to cite or link to this item: https://doi.org/10.21256/zhaw-22109
Publication type: Article in scientific journal
Type of review: Peer review (publication)
Title: The N-terminal region of Jaw1 has a role to inhibit the formation of organized smooth endoplasmic reticulum as an intrinsically disordered region
Authors: Kozono, Takuma
Sato, Hiroyuki
Okumura, Wataru
Jogano, Chifuyu
Tamura-Nakano, Miwa
Kawamura, Yuki I.
Rohrer, Jack
Tonozuka, Takashi
Nishikawa, Atsushi
et. al: No
DOI: 10.1038/s41598-020-80258-5
10.21256/zhaw-22109
Published in: Scientific Reports
Volume(Issue): 11
Issue: 753
Issue Date: 2021
Publisher / Ed. Institution: Nature Publishing Group
ISSN: 2045-2322
Language: English
Subjects: Organelles; Membrane structure and assembly; Intrinsically disordered protein
Subject (DDC): 572: Biochemistry
Abstract: Jaw1/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.
URI: https://digitalcollection.zhaw.ch/handle/11475/22109
Fulltext version: Published version
License (according to publishing contract): CC BY 4.0: Attribution 4.0 International
Departement: Life Sciences and Facility Management
Organisational Unit: Institute of Chemistry and Biotechnology (ICBT)
Appears in collections:Publikationen Life Sciences und Facility Management

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