ReviewNucleus (Austin, Tex.)
Membrane-coating lattice scaffolds in the nuclear pore and vesicle coats: commonalities, differences, challenges.
Review in Nucleus (Austin, Tex.). 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.
- GATOR2-dependent mTORC1 activity is a therapeutic vulnerability in FOXO1 fusion-positive rhabdomyosarcoma.JCI insight · 2022Article
- One Ring to Rule them All? Structural and Functional Diversity in the Nuclear Pore Complex.Trends in biochemical sciences · 2021Review
- Article
- Evolution of a transcriptional regulator from a transmembrane nucleoporin.Genes & development · 2016Article
- Structural characterization by cross-linking reveals the detailed architecture of a coatomer-related heptameric module from the nuclear pore complex.Molecular & cellular proteomics : MCP · 2014Article
- Integrative structure-function mapping of the nucleoporin Nup133 suggests a conserved mechanism for membrane anchoring of the nuclear pore complex.Molecular & cellular proteomics : MCP · 2014Article
- An inside-out origin for the eukaryotic cell.BMC biology · 2014Article
- The nuclear pore complex function of Sec13 protein is required for cell survival during retinal development.The Journal of biological chemistry · 2014Article
- A Tumor suppressor complex with GAP activity for the Rag GTPases that signal amino acid sufficiency to mTORC1.Science (New York, N.Y.) · 2013Article
- Evolution: functional evolution of nuclear structure.The Journal of cell biology · 2011Review
- A common mechanism for protein cluster formation.Small GTPases · 2011Article
- Characterization of human Sec16B: indications of specialized, non-redundant functions.Scientific reports · 2011Article
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Authors and funding
2 authors.
Funding
Abstract
The nuclear pore complex (NPC) regulates all traffic between the cytoplasm and the nucleus. It is a large protein assembly composed of multiple copies of ∼30 nucleoporins (nups). Structural studies of the NPC have been limited by its considerable size and complexity. Progress toward understanding the structure of this nanomachine has benefited from its modular nature, which allows for this 40-60 MDa assembly to be broken down into subcomplexes that can be studied individually. While recent work by both crystallographers and electron microscopists has greatly enhanced our model of the NPC, the resolution gap between crystal and EM structures remains too large to confidently place individual proteins within the context of the fully assembled NPC. In an effort to arrive at a veritable model of the NPC, we solved the structure of several scaffold nups and defined the ancestral coatomer element (ACE1) common to a set of nucleoporins and COPII vesicle coat proteins. Subsequently, we proposed a lattice-like model of the NPC, analogous to the COPII lattice, in which ACE1 proteins form the edge elements and β-propellers form the vertex elements. Here, we review our recent studies, speculate on how interactions between subcomplexes of the NPC are mediated, and outline the steps and challenges that lay ahead on the path to understanding this enormous assembly in molecular detail.
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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.