ArticleBiophysical journal2018
Molecular Insights into the Mechanisms of SUN1 Oligomerization in the Nuclear Envelope.
Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 48 citations in OpenAlex.
- Nuclear SUN2 coordinates endothelial cell-matrix interactions to regulate blood vessel homeostasis and barrier function.Angiogenesis · 2026Article
- Nuclear SUN2 coordinates endothelial cell-matrix interactions to regulate blood vessel homeostasis and barrier function.bioRxiv : the preprint server for biology · 2026Article
- Exome sequencing identifies known and candidate genes in hearing impairment in Cameroon.Communications medicine · 2026Article
- SUN5 forms a regular protein lattice reinforcing the sperm head-tail junction.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Chromosome movements in meiotic prophase: regulatory mechanisms and biological roles.Frontiers in cell and developmental biology · 2026Review
- Elevated SUN1 promotes migratory cell polarity defects through mechanically coupling microtubules to the nuclear lamina.Communications biology · 2025Article
- Active microtubule-actin cross-talk mediated by a nesprin-2G-kinesin complex.Science advances · 2025Article
- Nuclear Envelope Dynamics inCells · 2025Review
- SUN1 inhibits osteogenesis and promotes adipogenesis of human adipose-derived stem cells by regulating α-tubulin and CD36 expression.Journal of cellular and molecular medicine · 2024Article
- Life outside the LINC complex - Do SUN proteins have LINC-independent functions?BioEssays : news and reviews in molecular, cellular and developmental biology · 2024Review
- Article
- Life at the crossroads: the nuclear LINC complex and vascular mechanotransduction.Frontiers in physiology · 2024Review
- Force transmission and SUN-KASH higher-order assembly in the LINC complex models.Biophysical journal · 2023Article
- Building and breaking mechanical bridges between the nucleus and cytoskeleton: Regulation of LINC complex assembly and disassembly.Current opinion in cell biology · 2023Review
- Molecular insights into LINC complex architecture through the crystal structure of a luminal trimeric coiled-coil domain of SUN1.Frontiers in cell and developmental biology · 2023Article
- Nuclear mechanosignaling in striated muscle diseases.Frontiers in physiology · 2023Review
- Article
- Article
- SUN2 Modulates the Propagation of HSV-1.Journal of virology · 2022Article
- Emerin self-assembly and nucleoskeletal coupling regulate nuclear envelope mechanics against stress.Journal of cell science · 2022Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The LINC complex is found in a wide variety of organisms and is formed by the transluminal interaction between outer- and inner-nuclear-membrane KASH and SUN proteins, respectively. Most extensively studied are SUN1 and SUN2 proteins, which are widely expressed in mammals. Although SUN1 and SUN2 play functionally redundant roles in several cellular processes, more recent studies have revealed diverse and distinct functions for SUN1. While several recent in vitro structural studies have revealed the molecular details of various fragments of SUN2, no such structural information is available for SUN1. Herein, we conduct a systematic analysis of the molecular relationships between SUN1 and SUN2, highlighting key similarities and differences that could lead to clues into their distinct functions. We use a wide range of computational tools, including multiple sequence alignments, homology modeling, molecular docking, and molecular dynamic simulations, to predict structural differences between SUN1 and SUN2, with the goal of understanding the molecular mechanisms underlying SUN1 oligomerization in the nuclear envelope. Our simulations suggest that the structural model of SUN1 is stable in a trimeric state and that SUN1 trimers can associate through their SUN domains to form lateral complexes. We also ask whether SUN1 could adopt an inactive monomeric conformation as seen in SUN2. Our results imply that the KASH binding domain of SUN1 is also inhibited in monomeric SUN1 but through weaker interactions than in monomeric SUN2.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.