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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; Gromova, Kira; Puchkov, Dmytro; Robertson, Mark J.; MacGregor, Kylie A.; Tomlin, Nikolay; Pechstein, Arndt; Chau, Ngoc; Chircop, Megan; Sakoff, Jennette; Von Kries, Jens Peter; Saenger, Wolfram; Kräusslich, Hans Georg; Shupliakov, Oleg; Robinson, Phillip J.; McCluskey, Adam; Haucke, Volker.

In: Cell, Vol. 146, No. 3, 05.08.2011, p. 471-484.

Research output: Contribution to journal › Article › peer-review

Harvard

Von Kleist, L, Stahlschmidt, W, Bulut, H, Gromova, K, Puchkov, D, Robertson, MJ, MacGregor, KA, Tomlin, N, Pechstein, A, Chau, N, Chircop, M, Sakoff, J, Von Kries, JP, Saenger, W, Kräusslich, HG, 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, pp. 471-484. https://doi.org/10.1016/j.cell.2011.06.025

APA

Von Kleist, L., Stahlschmidt, W., Bulut, H., Gromova, K., Puchkov, D., Robertson, M. J., MacGregor, K. A., Tomlin, N., Pechstein, A., Chau, N., Chircop, M., Sakoff, J., Von Kries, J. P., Saenger, W., Kräusslich, H. G., Shupliakov, O., Robinson, P. J., McCluskey, A., & Haucke, V. (2011). Role of the clathrin terminal domain in regulating coated pit dynamics revealed by small molecule inhibition. Cell, 146(3), 471-484. https://doi.org/10.1016/j.cell.2011.06.025

Vancouver

Von Kleist L, Stahlschmidt W, Bulut H, Gromova 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 Aug 5;146(3):471-484. https://doi.org/10.1016/j.cell.2011.06.025

Author

Von Kleist, Lisa ; Stahlschmidt, Wiebke ; Bulut, Haydar ; Gromova, Kira ; Puchkov, Dmytro ; Robertson, Mark J. ; MacGregor, Kylie A. ; Tomlin, Nikolay ; Pechstein, Arndt ; Chau, Ngoc ; Chircop, Megan ; Sakoff, Jennette ; Von Kries, Jens Peter ; Saenger, Wolfram ; Kräusslich, Hans Georg ; Shupliakov, Oleg ; Robinson, Phillip J. ; McCluskey, Adam ; Haucke, Volker. / Role of the clathrin terminal domain in regulating coated pit dynamics revealed by small molecule inhibition. In: Cell. 2011 ; Vol. 146, No. 3. pp. 471-484.

BibTeX

@article{5ce354725157456886b007a6cc5f2090,
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.",
author = "{Von Kleist}, Lisa and Wiebke Stahlschmidt and Haydar Bulut and Kira Gromova and Dmytro Puchkov and Robertson, {Mark J.} and MacGregor, {Kylie A.} and Nikolay Tomlin and Arndt Pechstein and Ngoc Chau and Megan Chircop and Jennette Sakoff and {Von Kries}, {Jens Peter} and Wolfram Saenger and Kr{\"a}usslich, {Hans Georg} and Oleg Shupliakov and Robinson, {Phillip J.} and Adam McCluskey and Volker Haucke",
year = "2011",
month = aug,
day = "5",
doi = "10.1016/j.cell.2011.06.025",
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 - Gromova, Kira

AU - Puchkov, Dmytro

AU - Robertson, Mark J.

AU - MacGregor, Kylie A.

AU - Tomlin, Nikolay

AU - Pechstein, Arndt

AU - Chau, Ngoc

AU - Chircop, Megan

AU - Sakoff, Jennette

AU - Von Kries, Jens Peter

AU - Saenger, Wolfram

AU - Kräusslich, Hans Georg

AU - Shupliakov, Oleg

AU - Robinson, Phillip J.

AU - McCluskey, Adam

AU - Haucke, Volker

PY - 2011/8/5

Y1 - 2011/8/5

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.

UR - http://www.scopus.com/inward/record.url?scp=79961140522&partnerID=8YFLogxK

U2 - 10.1016/j.cell.2011.06.025

DO - 10.1016/j.cell.2011.06.025

M3 - Article

C2 - 21816279

AN - SCOPUS:79961140522

VL - 146

SP - 471

EP - 484

JO - Cell

JF - Cell

SN - 0092-8674

IS - 3

ER -

ID: 40829290