ArticleMolecular biology of the cell2015
Conservation of inner nuclear membrane targeting sequences in mammalian Pom121 and yeast Heh2 membrane proteins.
Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 27 citations in OpenAlex.
- Nuclear pore protein POM121 regulates subcellular localization and transcriptional activity of PPARγ.Cell death & disease · 2024Article
- Structure and Function of the Nuclear Pore Complex.Cold Spring Harbor perspectives in biology · 2022Review
- Recognition of the TDP-43 nuclear localization signal by importin α1/β.Cell reports · 2022Article
- Architecture of the linker-scaffold in the nuclear pore.Science (New York, N.Y.) · 2022Article
- Nucleoporins in cardiovascular disease.Journal of molecular and cellular cardiology · 2020Review
- Ran pathway-independent regulation of mitotic Golgi disassembly by Importin-α.Nature communications · 2019Article
- The Structure of the Nuclear Pore Complex (An Update).Annual review of biochemistry · 2019Review
- Targeting of LRRC59 to the Endoplasmic Reticulum and the Inner Nuclear Membrane.International journal of molecular sciences · 2019Article
- Article
- Three-dimensional context rather than NLS amino acid sequence determines importin α subtype specificity for RCC1.Nature communications · 2017Article
- Review
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
Endoplasmic reticulum-synthesized membrane proteins traffic through the nuclear pore complex (NPC) en route to the inner nuclear membrane (INM). Although many membrane proteins pass the NPC by simple diffusion, two yeast proteins, ScSrc1/ScHeh1 and ScHeh2, are actively imported. In these proteins, a nuclear localization signal (NLS) and an intrinsically disordered linker encode the sorting signal for recruiting the transport factors for FG-Nup and RanGTP-dependent transport through the NPC. Here we address whether a similar import mechanism applies in metazoans. We show that the (putative) NLSs of metazoan HsSun2, MmLem2, HsLBR, and HsLap2β are not sufficient to drive nuclear accumulation of a membrane protein in yeast, but the NLS from RnPom121 is. This NLS of Pom121 adapts a similar fold as the NLS of Heh2 when transport factor bound and rescues the subcellular localization and synthetic sickness of Heh2ΔNLS mutants. Consistent with the conservation of these NLSs, the NLS and linker of Heh2 support INM localization in HEK293T cells. The conserved features of the NLSs of ScHeh1, ScHeh2, and RnPom121 and the effective sorting of Heh2-derived reporters in human cells suggest that active import is conserved but confined to a small subset of INM proteins.
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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.