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Role of the clathrin terminal domain in regulating coated pit dynamics revealed by small molecule inhibition.

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Role of the clathrin terminal domain in regulating coated pit dynamics revealed by small molecule inhibition. / von Kleist, Lisa; Stahlschmidt, Wiebke; Bulut, Haydar; Brune, Kira; Puchkov, Dmytro; Robertson, Mark J; MacGregor, Kylie A; Tomilin, Nikolay; Tomlin, Nikolay; Pechstein, Arndt; Chau, Ngoc; Chircop, Megan; Sakoff, Jennette; Kries, von; Peter, Jens; Saenger, Wolfram; Kräusslich, Hans-Georg; Shupliakov, Oleg; Robinson, Phillip J; McCluskey, Adam; Haucke, Volker.

In: CELL, Vol. 146, No. 3, 3, 2011, p. 471-484.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

von Kleist, L, Stahlschmidt, W, Bulut, H, Brune, K, Puchkov, D, Robertson, MJ, MacGregor, KA, Tomilin, N, Tomlin, N, Pechstein, A, Chau, N, Chircop, M, Sakoff, J, Kries, V, Peter, J, Saenger, W, Kräusslich, H-G, Shupliakov, O, Robinson, PJ, McCluskey, A & Haucke, V 2011, 'Role of the clathrin terminal domain in regulating coated pit dynamics revealed by small molecule inhibition.', CELL, vol. 146, no. 3, 3, pp. 471-484. <http://www.ncbi.nlm.nih.gov/pubmed/21816279?dopt=Citation>

APA

von Kleist, L., Stahlschmidt, W., Bulut, H., Brune, K., Puchkov, D., Robertson, M. J., MacGregor, K. A., Tomilin, N., Tomlin, N., Pechstein, A., Chau, N., Chircop, M., Sakoff, J., Kries, V., Peter, J., Saenger, W., Kräusslich, H-G., Shupliakov, O., Robinson, P. J., ... Haucke, V. (2011). Role of the clathrin terminal domain in regulating coated pit dynamics revealed by small molecule inhibition. CELL, 146(3), 471-484. [3]. http://www.ncbi.nlm.nih.gov/pubmed/21816279?dopt=Citation

Vancouver

von Kleist L, Stahlschmidt W, Bulut H, Brune K, Puchkov D, Robertson MJ et al. Role of the clathrin terminal domain in regulating coated pit dynamics revealed by small molecule inhibition. CELL. 2011;146(3):471-484. 3.

Bibtex

@article{aea45665124541199d429a478b75f34e,
title = "Role of the clathrin terminal domain in regulating coated pit dynamics revealed by small molecule inhibition.",
abstract = "Clathrin-mediated endocytosis (CME) regulates many cell physiological processes such as the internalization of growth factors and receptors, entry of pathogens, and synaptic transmission. Within the endocytic network, clathrin functions as a central organizing platform for coated pit assembly and dissociation via its terminal domain (TD). We report the design and synthesis of two compounds named pitstops that selectively block endocytic ligand association with the clathrin TD as confirmed by X-ray crystallography. Pitstop-induced inhibition of clathrin TD function acutely interferes with receptor-mediated endocytosis, entry of HIV, and synaptic vesicle recycling. Endocytosis inhibition is caused by a dramatic increase in the lifetimes of clathrin coat components, including FCHo, clathrin, and dynamin, suggesting that the clathrin TD regulates coated pit dynamics. Pitstops provide new tools to address clathrin function in cell physiology with potential applications as inhibitors of virus and pathogen entry and as modulators of cell signaling.",
keywords = "Animals, Humans, Cells, Cultured, Mice, Endocytosis, Protein Structure, Tertiary, Signal Transduction, Crystallography, X-Ray, Adaptor Protein Complex 2/metabolism, Clathrin/*chemistry/*metabolism, Coated Pits, Cell-Membrane/drug effects/*metabolism, Cytological Techniques/*methods, Dynamins/metabolism, *Small Molecule Libraries, Synapses/metabolism/ultrastructure, Animals, Humans, Cells, Cultured, Mice, Endocytosis, Protein Structure, Tertiary, Signal Transduction, Crystallography, X-Ray, Adaptor Protein Complex 2/metabolism, Clathrin/*chemistry/*metabolism, Coated Pits, Cell-Membrane/drug effects/*metabolism, Cytological Techniques/*methods, Dynamins/metabolism, *Small Molecule Libraries, Synapses/metabolism/ultrastructure",
author = "{von Kleist}, Lisa and Wiebke Stahlschmidt and Haydar Bulut and Kira Brune and Dmytro Puchkov and Robertson, {Mark J} and MacGregor, {Kylie A} and Nikolay Tomilin and Nikolay Tomlin and Arndt Pechstein and Ngoc Chau and Megan Chircop and Jennette Sakoff and von Kries and Jens Peter and Wolfram Saenger and Hans-Georg Kr{\"a}usslich and Oleg Shupliakov and Robinson, {Phillip J} and Adam McCluskey and Volker Haucke",
year = "2011",
language = "English",
volume = "146",
pages = "471--484",
journal = "CELL",
issn = "0092-8674",
publisher = "Cell Press",
number = "3",

}

RIS

TY - JOUR

T1 - Role of the clathrin terminal domain in regulating coated pit dynamics revealed by small molecule inhibition.

AU - von Kleist, Lisa

AU - Stahlschmidt, Wiebke

AU - Bulut, Haydar

AU - Brune, Kira

AU - Puchkov, Dmytro

AU - Robertson, Mark J

AU - MacGregor, Kylie A

AU - Tomilin, Nikolay

AU - Tomlin, Nikolay

AU - Pechstein, Arndt

AU - Chau, Ngoc

AU - Chircop, Megan

AU - Sakoff, Jennette

AU - Kries, von

AU - Peter, Jens

AU - Saenger, Wolfram

AU - Kräusslich, Hans-Georg

AU - Shupliakov, Oleg

AU - Robinson, Phillip J

AU - McCluskey, Adam

AU - Haucke, Volker

PY - 2011

Y1 - 2011

N2 - Clathrin-mediated endocytosis (CME) regulates many cell physiological processes such as the internalization of growth factors and receptors, entry of pathogens, and synaptic transmission. Within the endocytic network, clathrin functions as a central organizing platform for coated pit assembly and dissociation via its terminal domain (TD). We report the design and synthesis of two compounds named pitstops that selectively block endocytic ligand association with the clathrin TD as confirmed by X-ray crystallography. Pitstop-induced inhibition of clathrin TD function acutely interferes with receptor-mediated endocytosis, entry of HIV, and synaptic vesicle recycling. Endocytosis inhibition is caused by a dramatic increase in the lifetimes of clathrin coat components, including FCHo, clathrin, and dynamin, suggesting that the clathrin TD regulates coated pit dynamics. Pitstops provide new tools to address clathrin function in cell physiology with potential applications as inhibitors of virus and pathogen entry and as modulators of cell signaling.

AB - Clathrin-mediated endocytosis (CME) regulates many cell physiological processes such as the internalization of growth factors and receptors, entry of pathogens, and synaptic transmission. Within the endocytic network, clathrin functions as a central organizing platform for coated pit assembly and dissociation via its terminal domain (TD). We report the design and synthesis of two compounds named pitstops that selectively block endocytic ligand association with the clathrin TD as confirmed by X-ray crystallography. Pitstop-induced inhibition of clathrin TD function acutely interferes with receptor-mediated endocytosis, entry of HIV, and synaptic vesicle recycling. Endocytosis inhibition is caused by a dramatic increase in the lifetimes of clathrin coat components, including FCHo, clathrin, and dynamin, suggesting that the clathrin TD regulates coated pit dynamics. Pitstops provide new tools to address clathrin function in cell physiology with potential applications as inhibitors of virus and pathogen entry and as modulators of cell signaling.

KW - Animals

KW - Humans

KW - Cells, Cultured

KW - Mice

KW - Endocytosis

KW - Protein Structure, Tertiary

KW - Signal Transduction

KW - Crystallography, X-Ray

KW - Adaptor Protein Complex 2/metabolism

KW - Clathrin/chemistry/metabolism

KW - Coated Pits, Cell-Membrane/drug effects/metabolism

KW - Cytological Techniques/methods

KW - Dynamins/metabolism

KW - Small Molecule Libraries

KW - Synapses/metabolism/ultrastructure

KW - Animals

KW - Humans

KW - Cells, Cultured

KW - Mice

KW - Endocytosis

KW - Protein Structure, Tertiary

KW - Signal Transduction

KW - Crystallography, X-Ray

KW - Adaptor Protein Complex 2/metabolism

KW - Clathrin/chemistry/metabolism

KW - Coated Pits, Cell-Membrane/drug effects/metabolism

KW - Cytological Techniques/methods

KW - Dynamins/metabolism

KW - Small Molecule Libraries

KW - Synapses/metabolism/ultrastructure

M3 - SCORING: Journal article

VL - 146

SP - 471

EP - 484

JO - CELL

JF - CELL

SN - 0092-8674

IS - 3

M1 - 3

ER -