SUNny Ways: The Role of the SUN-Domain Protein Mps3 Bridging Yeast Nuclear Organization and Lipid Homeostasis

Ponce, Maria Laura Sosa; Moradi-Fard, Sarah; Zaremberg, Vanina; Cobb, Jennifer A.

doi:10.3389/fgene.2020.00136

Cited by 7 publications

(5 citation statements)

References 94 publications

(121 reference statements)

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“…The characterisation of the mps3-AAA and mps3-S189A and -S190A mutants revealed that Mps3 localisation to NE (NE remodelling) plays a unique role in NE expansion in meiotic cells. NE-bound Mps3 may regulate NE growth by directly promoting lipid synthesis on NE or by importing lipids from the ER ( Sosa Ponce et al, 2020 ).…”

Section: Discussionmentioning

confidence: 99%

Phosphorylation of luminal region of the SUN-domain protein Mps3 promotes nuclear envelope localization during meiosis

Rao

Sato

Challa

et al. 2021

eLife

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During meiosis, protein ensembles in the nuclear envelope (NE) containing SUN- and KASH-domain proteins, called linker nucleocytoskeleton and cytoskeleton (LINC) complex, promote the chromosome motion. Yeast SUN-domain protein, Mps3, forms multiple meiosis-specific ensembles on NE, which show dynamic localisation for chromosome motion; however, the mechanism by which these Mps3 ensembles are formed during meiosis remains largely unknown. Here, we showed that the cyclin-dependent protein kinase (CDK) and Dbf4-dependent Cdc7 protein kinase (DDK) regulate meiosis-specific dynamics of Mps3 on NE, particularly by mediating the resolution of Mps3 clusters and telomere clustering. We also found that the luminal region of Mps3 juxtaposed to the inner nuclear membrane is required for meiosis-specific localisation of Mps3 on NE. Negative charges introduced by meiosis-specific phosphorylation in the luminal region of Mps3 alter its interaction with negatively charged lipids by electric repulsion in reconstituted liposomes. Phospho-mimetic substitution in the luminal region suppresses the localisation of Mps3 via the inactivation of CDK or DDK. Our study revealed multi-layered phosphorylation-dependent regulation of the localisation of Mps3 on NE for meiotic chromosome motion and NE remodelling.

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Section: Discussionmentioning

confidence: 99%

Phosphorylation of luminal region of the SUN-domain protein Mps3 promotes nuclear envelope localization during meiosis

Rao

Sato

Challa

et al. 2021

eLife

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“…SUN1/2 are expressed in skeletal and cardiac muscles in humans ( Crisp et al, 2006 ; Puckelwartz et al, 2009 ; Zhang et al, 2010 ). They both have a C-terminal SUN domain, a coiled-coil domain, a transmembrane (TM) domain, and an N-terminus nucleoplasmic domain ( Stroud, 2018 ; Sosa Ponce et al, 2020 ). The SUN domain is the most conserved domain that interacts with the KASH domain on Nesprin ( Sosa et al, 2012 ; Wang et al, 2012 ; Sosa Ponce et al, 2020 ).…”

Section: Functions Of Nuclear Envelope and Nucleoskeleton Proteins In...mentioning

confidence: 99%

“…They both have a C-terminal SUN domain, a coiled-coil domain, a transmembrane (TM) domain, and an N-terminus nucleoplasmic domain ( Stroud, 2018 ; Sosa Ponce et al, 2020 ). The SUN domain is the most conserved domain that interacts with the KASH domain on Nesprin ( Sosa et al, 2012 ; Wang et al, 2012 ; Sosa Ponce et al, 2020 ). Inter-protein interactions between the coiled-coil domains form the SUN protein trimer ( Sosa et al, 2012 ; Jahed et al, 2018a ; Jahed et al, 2018b ; Sosa Ponce et al, 2020 ).…”

Section: Functions Of Nuclear Envelope and Nucleoskeleton Proteins In...mentioning

confidence: 99%

“…The SUN domain is the most conserved domain that interacts with the KASH domain on Nesprin ( Sosa et al, 2012 ; Wang et al, 2012 ; Sosa Ponce et al, 2020 ). Inter-protein interactions between the coiled-coil domains form the SUN protein trimer ( Sosa et al, 2012 ; Jahed et al, 2018a ; Jahed et al, 2018b ; Sosa Ponce et al, 2020 ). The N-terminus nucleoplasm domain binds with emerin and lamin A/C, anchoring the SUN protein at the NE ( Crisp et al, 2006 ; Haque et al, 2010 ).…”

Section: Functions Of Nuclear Envelope and Nucleoskeleton Proteins In...mentioning

confidence: 99%

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Nuclear mechanosignaling in striated muscle diseases

Zhang

Powers²,

McCulloch³

et al. 2023

Front. Physiol.

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Mechanosignaling describes processes by which biomechanical stimuli are transduced into cellular responses. External biophysical forces can be transmitted via structural protein networks that span from the cellular membrane to the cytoskeleton and the nucleus, where they can regulate gene expression through a series of biomechanical and/or biochemical mechanosensitive mechanisms, including chromatin remodeling, translocation of transcriptional regulators, and epigenetic factors. Striated muscle cells, including cardiac and skeletal muscle myocytes, utilize these nuclear mechanosignaling mechanisms to respond to changes in their intracellular and extracellular mechanical environment and mediate gene expression and cell remodeling. In this brief review, we highlight and discuss recent experimental work focused on the pathway of biomechanical stimulus propagation at the nucleus-cytoskeleton interface of striated muscles, and the mechanisms by which these pathways regulate gene regulation, muscle structure, and function. Furthermore, we discuss nuclear protein mutations that affect mechanosignaling function in human and animal models of cardiomyopathy. Furthermore, current open questions and future challenges in investigating striated muscle nuclear mechanosignaling are further discussed.

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“…Interestingly, the LINC and the SPB spatially co-localize in mitotic cells, whereas the LINC only spreads over the NE in meiosis, where it forms a specialized complex that connects telomeres to the cytoskeleton [ 38 ]. Mutants for both the LINC and SPBs share phenotypes of misshapen nuclei [ 39 ]. In addition, NPC mutants also lead to impressive aberrant NE morphologies as well [ 40 ].…”

Section: The Yeast Nucleus: a Model To Address Nuclear Morphology And...mentioning

confidence: 99%

A Yeast Mitotic Tale for the Nucleus and the Vacuoles to Embrace

Santana-Sosa

Matos-Perdomo

Ayra-Plasencia

et al. 2023

IJMS

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The morphology of the nucleus is roughly spherical in most eukaryotic cells. However, this organelle shape needs to change as the cell travels through narrow intercellular spaces during cell migration and during cell division in organisms that undergo closed mitosis, i.e., without dismantling the nuclear envelope, such as yeast. In addition, the nuclear morphology is often modified under stress and in pathological conditions, being a hallmark of cancer and senescent cells. Thus, understanding nuclear morphological dynamics is of uttermost importance, as pathways and proteins involved in nuclear shaping can be targeted in anticancer, antiaging, and antifungal therapies. Here, we review how and why the nuclear shape changes during mitotic blocks in yeast, introducing novel data that associate these changes with both the nucleolus and the vacuole. Altogether, these findings suggest a close relationship between the nucleolar domain of the nucleus and the autophagic organelle, which we also discuss here. Encouragingly, recent evidence in tumor cell lines has linked aberrant nuclear morphology to defects in lysosomal function.

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SUNny Ways: The Role of the SUN-Domain Protein Mps3 Bridging Yeast Nuclear Organization and Lipid Homeostasis

Cited by 7 publications

References 94 publications

Phosphorylation of luminal region of the SUN-domain protein Mps3 promotes nuclear envelope localization during meiosis

Phosphorylation of luminal region of the SUN-domain protein Mps3 promotes nuclear envelope localization during meiosis

Nuclear mechanosignaling in striated muscle diseases

A Yeast Mitotic Tale for the Nucleus and the Vacuoles to Embrace

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