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Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self-assembly

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Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self-assembly. / Morris, Kyle L; Jones, Joseph R; Halebian, Mary ; Wu, Shenping; Baker, Michael; Armache, Jean-Paul; Avila Ibarra, Amaurys; Sessions, Richard B; Cameron, Alexander D; Cheng, Yifan; Smith, Corinne J I.

In: Nature Structural and Molecular Biology, Vol. 26, 03.10.2019, p. 890-898.

Research output: Contribution to journalArticle

Harvard

Morris, KL, Jones, JR, Halebian, M, Wu, S, Baker, M, Armache, J-P, Avila Ibarra, A, Sessions, RB, Cameron, AD, Cheng, Y & Smith, CJI 2019, 'Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self-assembly', Nature Structural and Molecular Biology, vol. 26, pp. 890-898. https://doi.org/10.1038/s41594-019-0292-0

APA

Morris, K. L., Jones, J. R., Halebian, M., Wu, S., Baker, M., Armache, J-P., ... Smith, C. J. I. (2019). Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self-assembly. Nature Structural and Molecular Biology, 26, 890-898. https://doi.org/10.1038/s41594-019-0292-0

Vancouver

Morris KL, Jones JR, Halebian M, Wu S, Baker M, Armache J-P et al. Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self-assembly. Nature Structural and Molecular Biology. 2019 Oct 3;26:890-898. https://doi.org/10.1038/s41594-019-0292-0

Author

Morris, Kyle L ; Jones, Joseph R ; Halebian, Mary ; Wu, Shenping ; Baker, Michael ; Armache, Jean-Paul ; Avila Ibarra, Amaurys ; Sessions, Richard B ; Cameron, Alexander D ; Cheng, Yifan ; Smith, Corinne J I. / Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self-assembly. In: Nature Structural and Molecular Biology. 2019 ; Vol. 26. pp. 890-898.

Bibtex

@article{ea64dc5b11d54e9fa90ce6398fb2aa23,
title = "Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self-assembly",
abstract = "Clathrin forms diverse lattice and cage structures that change size and shape rapidly in response to the needs of eukaryotic cells during clathrin-mediated endocytosis and intracellular trafficking. We present the cryo-EM structure and molecular model of assembled porcine clathrin, providing insights into interactions that stabilize key elements of the clathrin lattice, namely, between adjacent heavy chains, at the light chain–heavy chain interface and within the trimerization domain. Furthermore, we report cryo-EM maps for five different clathrin cage architectures. Fitting structural models to three of these maps shows that their assembly requires only a limited range of triskelion leg conformations, yet inherent flexibility is required to maintain contacts. Analysis of the protein–protein interfaces shows remarkable conservation of contact sites despite architectural variation. These data reveal a universal mode of clathrin assembly that allows variable cage architecture and adaptation of coated vesicle size and shape during clathrin-mediated vesicular trafficking or endocytosis.",
keywords = "cryoelectron microscopy, membrane curvature, membrane trafficking, proteins",
author = "Morris, {Kyle L} and Jones, {Joseph R} and Mary Halebian and Shenping Wu and Michael Baker and Jean-Paul Armache and {Avila Ibarra}, Amaurys and Sessions, {Richard B} and Cameron, {Alexander D} and Yifan Cheng and Smith, {Corinne J I}",
year = "2019",
month = "10",
day = "3",
doi = "10.1038/s41594-019-0292-0",
language = "English",
volume = "26",
pages = "890--898",
journal = "Nature Structural and Molecular Biology",
issn = "1545-9993",
publisher = "Springer Nature",

}

RIS - suitable for import to EndNote

TY - JOUR

T1 - Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self-assembly

AU - Morris, Kyle L

AU - Jones, Joseph R

AU - Halebian, Mary

AU - Wu, Shenping

AU - Baker, Michael

AU - Armache, Jean-Paul

AU - Avila Ibarra, Amaurys

AU - Sessions, Richard B

AU - Cameron, Alexander D

AU - Cheng, Yifan

AU - Smith, Corinne J I

PY - 2019/10/3

Y1 - 2019/10/3

N2 - Clathrin forms diverse lattice and cage structures that change size and shape rapidly in response to the needs of eukaryotic cells during clathrin-mediated endocytosis and intracellular trafficking. We present the cryo-EM structure and molecular model of assembled porcine clathrin, providing insights into interactions that stabilize key elements of the clathrin lattice, namely, between adjacent heavy chains, at the light chain–heavy chain interface and within the trimerization domain. Furthermore, we report cryo-EM maps for five different clathrin cage architectures. Fitting structural models to three of these maps shows that their assembly requires only a limited range of triskelion leg conformations, yet inherent flexibility is required to maintain contacts. Analysis of the protein–protein interfaces shows remarkable conservation of contact sites despite architectural variation. These data reveal a universal mode of clathrin assembly that allows variable cage architecture and adaptation of coated vesicle size and shape during clathrin-mediated vesicular trafficking or endocytosis.

AB - Clathrin forms diverse lattice and cage structures that change size and shape rapidly in response to the needs of eukaryotic cells during clathrin-mediated endocytosis and intracellular trafficking. We present the cryo-EM structure and molecular model of assembled porcine clathrin, providing insights into interactions that stabilize key elements of the clathrin lattice, namely, between adjacent heavy chains, at the light chain–heavy chain interface and within the trimerization domain. Furthermore, we report cryo-EM maps for five different clathrin cage architectures. Fitting structural models to three of these maps shows that their assembly requires only a limited range of triskelion leg conformations, yet inherent flexibility is required to maintain contacts. Analysis of the protein–protein interfaces shows remarkable conservation of contact sites despite architectural variation. These data reveal a universal mode of clathrin assembly that allows variable cage architecture and adaptation of coated vesicle size and shape during clathrin-mediated vesicular trafficking or endocytosis.

KW - cryoelectron microscopy

KW - membrane curvature

KW - membrane trafficking

KW - proteins

UR - http://www.scopus.com/inward/record.url?scp=85072937933&partnerID=8YFLogxK

U2 - 10.1038/s41594-019-0292-0

DO - 10.1038/s41594-019-0292-0

M3 - Article

VL - 26

SP - 890

EP - 898

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

SN - 1545-9993

ER -