Jaw1/LRMP has a role in maintaining nuclear shape via interaction with SUN proteins

Kozono, Takuma; Tadahira, Kazuko; Okumura, Wataru; Itai, Nao; Tamura‐Nakano, Miwa; Dohi, Taeko; Tonozuka, Takashi; Nishikawa, Atsushi

doi:10.1093/jb/mvy053

Cited by 29 publications

(55 citation statements)

References 35 publications

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“…Jaw1 coiled-coil domain is a candidate for the oligomerization site. As we previously reported, Jaw1 plays a role in maintaining the nuclear shape as a KASH protein in the state of oligomer 28 . However, the oligomerization site has not been identified.…”

Section: Resultsmentioning

confidence: 51%

“…Intriguingly, some KASH proteins such as Nesprin3α and KASH5 have been reported to be oligomerized via their cytosolic regions to stabilize the interaction with proteins 27,34 . As we previously reported, Jaw1 also forms an oligomer, but the issue of whether or not the oligomerization is mediated by its cytosolic region has not been revealed 28 . Furthermore, Jaw1 has a predicted coiled-coil domain in the middle region on its cytosolic face which interacts with the type III inositol 1,4,5-triphosphate receptor (IP 3 R3), a calcium-gate channel on the ER membrane 26,30 .…”

mentioning

confidence: 87%

“…Jaw1 is a type II integral membrane protein that is localized on the ER and ONM [26][27][28] . Current information indicates that Jaw1 is expressed in taste buds and lymphoid organs such as the spleen, thymus, bone marrow and tonsils 26,29,30 .…”

mentioning

confidence: 99%

“…Current information indicates that Jaw1 is expressed in taste buds and lymphoid organs such as the spleen, thymus, bone marrow and tonsils 26,29,30 . We recently reported that Jaw1 has a role in maintaining the nuclear shape at ONM as a KASH protein 28 . Trimeric KASH proteins interact with trimeric SUN proteins in the perinuclear space (PNS) via the KASH domain and the SUN domain, respectively, resulting in the formation of a hetero-hexamer complex [31][32][33] .…”

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confidence: 99%

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

Kozono

Sato

Okumura

et al. 2021

Sci Rep

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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.

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Section: Resultsmentioning

confidence: 51%

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confidence: 87%

mentioning

confidence: 99%

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confidence: 99%

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

Kozono

Sato

Okumura

et al. 2021

Sci Rep

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“…In zebrafish and likely human embryos, Lrmp1/KASH5 plays an analogous role to ZYG-12, recruiting dynein to nuclei to mediate pronuclear migration. 88,103…”

Section: Sun-1/zyg-12 Linc Complexes Mediate Pronuclear Migration In mentioning

confidence: 99%

A network of nuclear envelope proteins and cytoskeletal force generators mediates movements of and within nuclei throughoutCaenorhabditis elegansdevelopment

Starr

2019

Exp Biol Med (Maywood)

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Nuclear migration and anchorage, together referred to as nuclear positioning, are central to many cellular and developmental events. Nuclear positioning is mediated by a conserved network of nuclear envelope proteins that interacts with force generators in the cytoskeleton. At the heart of this network are linker of nucleoskeleton and cytoskeleton (LINC) complexes made of Sad1 and UNC-84 (SUN) proteins at the inner nuclear membrane and Klarsicht, ANC-1, and Syne homology (KASH) proteins in the outer nuclear membrane. LINC complexes span the nuclear envelope, maintain nuclear envelope architecture, designate the surface of nuclei distinctly from the contiguous endoplasmic reticulum, and were instrumental in the early evolution of eukaryotes. LINC complexes interact with lamins in the nucleus and with various cytoplasmic KASH effectors from the surface of nuclei. These effectors regulate the cytoskeleton, leading to a variety of cellular outputs including pronuclear migration, nuclear migration through constricted spaces, nuclear anchorage, centrosome attachment to nuclei, meiotic chromosome movements, and DNA damage repair. How LINC complexes are regulated and how they function are reviewed here. The focus is on recent studies elucidating the best-understood network of LINC complexes, those used throughout Caenorhabditis elegans development. Impact statement Defects in nuclear positioning disrupt development in many mammalian tissues. In human development, LINC complexes play important cellular functions including nuclear positioning, homolog pairing in meiosis, DNA damage repair, wound healing, and gonadogenesis. The topics reviewed here are relevant to public health because defects in nuclear positioning and mutations in LINC components are associated with a wide variety of human diseases including muscular dystrophies, neurological disorders, progeria, aneurysms, hearing loss, blindness, sterility, and multiple cancers. Although this review focuses on findings in the model nematode Caenorhabditis elegans, the studies are relevant because almost all the findings originally made in C. elegans are conserved to humans. Furthermore, C. elegans remains the best described network for how LINC complexes are regulated and function.

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Life outside the LINC complex – Do SUN proteins have LINC‐independent functions?

Belaadi,

Guilluy

2024

BioEssays

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Sad1 and UNC84 (SUN) and Klarsicht, ANC‐1, and Syne homology (KASH) proteins interact at the nuclear periphery to form the linker of nucleoskeleton and cytoskeleton (LINC) complex, spanning the nuclear envelope (NE) and connecting the cytoskeleton with the nuclear interior. It is now well‐documented that several cellular functions depend on LINC complex formation, including cell differentiation and migration. Intriguingly, recent studies suggest that SUN proteins participate in cellular processes where their association with KASH proteins may not be required. Building on this recent research, we elaborate on the hypothesis that SUN proteins may perform LINC‐independent functions and discuss the modalities that may allow SUN proteins to function at the INM when they are not forming LINC complex.

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Jaw1/LRMP has a role in maintaining nuclear shape via interaction with SUN proteins

Cited by 29 publications

References 35 publications

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

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

A network of nuclear envelope proteins and cytoskeletal force generators mediates movements of and within nuclei throughoutCaenorhabditis elegansdevelopment

Life outside the LINC complex – Do SUN proteins have LINC‐independent functions?

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