The N-terminal region of Jaw1 has a role to inhibit the formation of organized smooth endoplasmic reticulum as an intrinsically disordered region

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 nucle...

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Autores principales: Takuma Kozono, Hiroyuki Sato, Wataru Okumura, Chifuyu Jogano, Miwa Tamura-Nakano, Yuki I. Kawamura, Jack Rohrer, Takashi Tonozuka, Atsushi Nishikawa
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Publicado: Nature Portfolio 2021
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spelling oai:doaj.org-article:9b0bbb77d4e84230962f6a8b257e98b92021-12-02T14:12:40ZThe N-terminal region of Jaw1 has a role to inhibit the formation of organized smooth endoplasmic reticulum as an intrinsically disordered region10.1038/s41598-020-80258-52045-2322https://doaj.org/article/9b0bbb77d4e84230962f6a8b257e98b92021-01-01T00:00:00Zhttps://doi.org/10.1038/s41598-020-80258-5https://doaj.org/toc/2045-2322Abstract 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.Takuma KozonoHiroyuki SatoWataru OkumuraChifuyu JoganoMiwa Tamura-NakanoYuki I. KawamuraJack RohrerTakashi TonozukaAtsushi NishikawaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-17 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Takuma Kozono
Hiroyuki Sato
Wataru Okumura
Chifuyu Jogano
Miwa Tamura-Nakano
Yuki I. Kawamura
Jack Rohrer
Takashi Tonozuka
Atsushi Nishikawa
The N-terminal region of Jaw1 has a role to inhibit the formation of organized smooth endoplasmic reticulum as an intrinsically disordered region
description 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.
format article
author Takuma Kozono
Hiroyuki Sato
Wataru Okumura
Chifuyu Jogano
Miwa Tamura-Nakano
Yuki I. Kawamura
Jack Rohrer
Takashi Tonozuka
Atsushi Nishikawa
author_facet Takuma Kozono
Hiroyuki Sato
Wataru Okumura
Chifuyu Jogano
Miwa Tamura-Nakano
Yuki I. Kawamura
Jack Rohrer
Takashi Tonozuka
Atsushi Nishikawa
author_sort Takuma Kozono
title The N-terminal region of Jaw1 has a role to inhibit the formation of organized smooth endoplasmic reticulum as an intrinsically disordered region
title_short The N-terminal region of Jaw1 has a role to inhibit the formation of organized smooth endoplasmic reticulum as an intrinsically disordered region
title_full The N-terminal region of Jaw1 has a role to inhibit the formation of organized smooth endoplasmic reticulum as an intrinsically disordered region
title_fullStr The N-terminal region of Jaw1 has a role to inhibit the formation of organized smooth endoplasmic reticulum as an intrinsically disordered region
title_full_unstemmed The N-terminal region of Jaw1 has a role to inhibit the formation of organized smooth endoplasmic reticulum as an intrinsically disordered region
title_sort n-terminal region of jaw1 has a role to inhibit the formation of organized smooth endoplasmic reticulum as an intrinsically disordered region
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/9b0bbb77d4e84230962f6a8b257e98b9
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