ArticleCommunicative & integrative biology2011
FG repeats facilitate integral protein trafficking to the inner nuclear membrane.
Article in Communicative & integrative biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Unveiling the complexity: assessing models describing the structure and function of the nuclear pore complex.Frontiers in cell and developmental biology · 2023Review
- Invasion and Propagation of White Spot Syndrome Virus: Hijacking of the Cytoskeleton, Intracellular Transport Machinery, and Nuclear Import Transporters.Journal of virology · 2022Article
- Super-resolution 3D tomography of interactions and competition in the nuclear pore complex.Nature structural & molecular biology · 2016Article
- Nuclear membrane diversity: underlying tissue-specific pathologies in disease?Current opinion in cell biology · 2015Review
- Many mechanisms, one entrance: membrane protein translocation into the nucleus.Cellular and molecular life sciences : CMLS · 2012Review
- Tissue specificity in the nuclear envelope supports its functional complexity.Nucleus (Austin, Tex.)Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The mechanism for nucleo-cytoplasmic transport of integral membrane proteins is poorly understood compared to transport of soluble molecules. We recently demonstrated that at least four distinct mechanisms can contribute to transport of integral proteins through the peripheral channels of the nuclear pore complex. One of these requires having multiple phenylalanine-glycine (FG) pairings on the integral protein. It also requires the nuclear pore complex protein Nup35, which separately contains FG repeats. FG-repeats on nuclear pore complex proteins in the central channel have been proposed to interact with FGs on transport receptors to facilitate transport of soluble proteins. Here we show that FG repeats occur quite frequently in both transmembrane and soluble proteins identified in multiple separate proteomic analyses of nuclear envelopes. We postulate that the FG repeats enable these proteins to function as their own transport receptors.
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Registered trials
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