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Docking a flexible basket onto the core of the nuclear pore complex
by
Stankunas, Edvinas
, Köhler, Alwin
in
14/28
/ 14/34
/ 14/35
/ 14/63
/ 631/337/386/1700
/ 631/45/612/1245
/ 631/535/1258
/ 631/80/389/2029
/ 82/16
/ 82/58
/ 82/80
/ 82/83
/ Biomedical and Life Sciences
/ Cancer Research
/ Cell Biology
/ Developmental Biology
/ Docks
/ Electron microscopy
/ Harbors
/ Heterogeneity
/ Life Sciences
/ Membranes
/ Microscopy
/ Nuclear Pore - genetics
/ Nuclear Pore - metabolism
/ Nuclear Pore - ultrastructure
/ Nuclear Pore Complex Proteins - chemistry
/ Nuclear Pore Complex Proteins - genetics
/ Nuclear Pore Complex Proteins - metabolism
/ Nuclear pores
/ Protein Binding
/ Protein structure
/ Protein transport
/ Proteins
/ Quality control
/ RNA transport
/ Saccharomyces cerevisiae - genetics
/ Saccharomyces cerevisiae - metabolism
/ Saccharomyces cerevisiae Proteins - chemistry
/ Saccharomyces cerevisiae Proteins - genetics
/ Saccharomyces cerevisiae Proteins - metabolism
/ Screens
/ Stem Cells
/ Structure-function relationships
2024
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Docking a flexible basket onto the core of the nuclear pore complex
by
Stankunas, Edvinas
, Köhler, Alwin
in
14/28
/ 14/34
/ 14/35
/ 14/63
/ 631/337/386/1700
/ 631/45/612/1245
/ 631/535/1258
/ 631/80/389/2029
/ 82/16
/ 82/58
/ 82/80
/ 82/83
/ Biomedical and Life Sciences
/ Cancer Research
/ Cell Biology
/ Developmental Biology
/ Docks
/ Electron microscopy
/ Harbors
/ Heterogeneity
/ Life Sciences
/ Membranes
/ Microscopy
/ Nuclear Pore - genetics
/ Nuclear Pore - metabolism
/ Nuclear Pore - ultrastructure
/ Nuclear Pore Complex Proteins - chemistry
/ Nuclear Pore Complex Proteins - genetics
/ Nuclear Pore Complex Proteins - metabolism
/ Nuclear pores
/ Protein Binding
/ Protein structure
/ Protein transport
/ Proteins
/ Quality control
/ RNA transport
/ Saccharomyces cerevisiae - genetics
/ Saccharomyces cerevisiae - metabolism
/ Saccharomyces cerevisiae Proteins - chemistry
/ Saccharomyces cerevisiae Proteins - genetics
/ Saccharomyces cerevisiae Proteins - metabolism
/ Screens
/ Stem Cells
/ Structure-function relationships
2024
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Docking a flexible basket onto the core of the nuclear pore complex
by
Stankunas, Edvinas
, Köhler, Alwin
in
14/28
/ 14/34
/ 14/35
/ 14/63
/ 631/337/386/1700
/ 631/45/612/1245
/ 631/535/1258
/ 631/80/389/2029
/ 82/16
/ 82/58
/ 82/80
/ 82/83
/ Biomedical and Life Sciences
/ Cancer Research
/ Cell Biology
/ Developmental Biology
/ Docks
/ Electron microscopy
/ Harbors
/ Heterogeneity
/ Life Sciences
/ Membranes
/ Microscopy
/ Nuclear Pore - genetics
/ Nuclear Pore - metabolism
/ Nuclear Pore - ultrastructure
/ Nuclear Pore Complex Proteins - chemistry
/ Nuclear Pore Complex Proteins - genetics
/ Nuclear Pore Complex Proteins - metabolism
/ Nuclear pores
/ Protein Binding
/ Protein structure
/ Protein transport
/ Proteins
/ Quality control
/ RNA transport
/ Saccharomyces cerevisiae - genetics
/ Saccharomyces cerevisiae - metabolism
/ Saccharomyces cerevisiae Proteins - chemistry
/ Saccharomyces cerevisiae Proteins - genetics
/ Saccharomyces cerevisiae Proteins - metabolism
/ Screens
/ Stem Cells
/ Structure-function relationships
2024
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Docking a flexible basket onto the core of the nuclear pore complex
Journal Article
Docking a flexible basket onto the core of the nuclear pore complex
2024
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Overview
The nuclear basket attaches to the nucleoplasmic side of the nuclear pore complex (NPC), coupling transcription to mRNA quality control and export. The basket expands the functional repertoire of a subset of NPCs in
Saccharomyces cerevisiae
by drawing a unique RNA/protein interactome. Yet, how the basket docks onto the NPC core remains unknown. By integrating AlphaFold-based interaction screens, electron microscopy and membrane-templated reconstitution, we uncovered a membrane-anchored tripartite junction between basket and NPC core. The basket subunit Nup60 harbours three adjacent short linear motifs, which connect Mlp1, a parallel homodimer consisting of coiled-coil segments interrupted by flexible hinges, and the Nup85 subunit of the Y-complex. We reconstituted the Y-complex•Nup60•Mlp1 assembly on a synthetic membrane and validated the protein interfaces in vivo. Here we explain how a short linear motif-based protein junction can substantially reshape NPC structure and function, advancing our understanding of compositional and conformational NPC heterogeneity.
Stankunas and Köhler define how the nucleoplasmic portion of the nuclear pore complex (NPC), the basket, docks onto the NPC core by integrating AlphaFold-based interaction screens, electron microscopy, and membrane-templated reconstitutions.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 14/34
/ 14/35
/ 14/63
/ 82/16
/ 82/58
/ 82/80
/ 82/83
/ Biomedical and Life Sciences
/ Docks
/ Harbors
/ Nuclear Pore - ultrastructure
/ Nuclear Pore Complex Proteins - chemistry
/ Nuclear Pore Complex Proteins - genetics
/ Nuclear Pore Complex Proteins - metabolism
/ Proteins
/ Saccharomyces cerevisiae - genetics
/ Saccharomyces cerevisiae - metabolism
/ Saccharomyces cerevisiae Proteins - chemistry
/ Saccharomyces cerevisiae Proteins - genetics
/ Saccharomyces cerevisiae Proteins - metabolism
/ Screens
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