{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T16:34:30Z","timestamp":1791304470279,"version":"4.3.1"},"reference-count":65,"publisher":"Rockefeller University Press","issue":"4","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2014,2,17]]},"abstract":"<jats:p>In closed mitotic systems such as Saccharomyces cerevisiae, nuclear pore complexes (NPCs) and the spindle pole body (SPB) must assemble into an intact nuclear envelope (NE). Ndc1 is a highly conserved integral membrane protein involved in insertion of both complexes. In this study, we show that Ndc1 interacts with the SUN domain\u2013containing protein Mps3 on the NE in live yeast cells using fluorescence cross-correlation spectroscopy. Genetic and molecular analysis of a series of new ndc1 alleles allowed us to understand the role of Ndc1\u2013Mps3 binding at the NE. We show that the ndc1-L562S allele is unable to associate specifically with Mps3 and find that this mutant is lethal due to a defect in SPB duplication. Unlike other ndc1 alleles, the growth and Mps3 binding defect of ndc1-L562S is fully suppressed by deletion of POM152, which encodes a NPC component. Based on our data we propose that the Ndc1\u2013Mps3 interaction is important for controlling the distribution of Ndc1 between the NPC and SPB.<\/jats:p>","DOI":"10.1083\/jcb.201307043","type":"journal-article","created":{"date-parts":[[2014,2,11]],"date-time":"2014-02-11T04:39:46Z","timestamp":1392093586000},"page":"523-539","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":51,"title":["The SUN protein Mps3 controls Ndc1 distribution and function on the nuclear membrane"],"prefix":"10.1083","volume":"204","author":[{"given":"Jingjing","family":"Chen","sequence":"first","affiliation":[{"name":"Stowers Institute for Medical Research, Kansas City, MO 64110 1"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christine J.","family":"Smoyer","sequence":"additional","affiliation":[{"name":"Stowers Institute for Medical Research, Kansas City, MO 64110 1"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brian D.","family":"Slaughter","sequence":"additional","affiliation":[{"name":"Stowers Institute for Medical Research, Kansas City, MO 64110 1"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jay R.","family":"Unruh","sequence":"additional","affiliation":[{"name":"Stowers Institute for Medical Research, Kansas City, MO 64110 1"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sue L.","family":"Jaspersen","sequence":"additional","affiliation":[{"name":"Stowers Institute for Medical Research, Kansas City, MO 64110 1"},{"name":"Department of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, KS 66160 2"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"291","published-online":{"date-parts":[[2014,2,10]]},"reference":[{"key":"2023072306290304800_bib1","doi-asserted-by":"publisher","first-page":"855","DOI":"10.1534\/genetics.111.127803","article-title":"The yeast nuclear pore complex and transport through it","volume":"190","author":"Aitchison","year":"2012","journal-title":"Genetics."},{"key":"2023072306290304800_bib2","doi-asserted-by":"publisher","first-page":"683","DOI":"10.1038\/nature06404","article-title":"Determining the architectures of macromolecular assemblies","volume":"450","author":"Alber","year":"2007","journal-title":"Nature."},{"key":"2023072306290304800_bib3","doi-asserted-by":"publisher","first-page":"1959","DOI":"10.1091\/mbc.E05-07-0668","article-title":"The Saccharomyces cerevisiae spindle pole body (SPB) component Nbp1p is required for SPB membrane insertion and interacts with the integral membrane proteins Ndc1p and Mps2p","volume":"17","author":"Araki","year":"2006","journal-title":"Mol. 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