Ripping up the nuclear envelope

Lippincott‐Schwartz, Jennifer

doi:10.1038/416031a

Cited by 23 publications

(15 citation statements)

References 14 publications

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“…However, another possibility is suggested by the presence of L2 in the ER. Components of the nuclear envelope redistribute into the ER upon nuclear envelope breakdown during mitosis (47, 48). The ER then serves as the source of membrane material for reassembly of the nuclear envelope when mitosis is complete.…”

Section: Discussionmentioning

confidence: 99%

Vesicular Trafficking of Incoming Human Papillomavirus 16 to the Golgi Apparatus and Endoplasmic Reticulum Requires γ-Secretase Activity

Zhang

Kazakov

Popa

et al. 2014

mBio

128

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The route taken by papillomaviruses from the cell surface to the nucleus during infection is incompletely understood. Here, we developed a novel human papillomavirus 16 (HPV16) pseudovirus in which the carboxy terminus of the minor capsid protein L2 is exposed on the exterior of the intact capsid prior to cell binding. With this pseudovirus, we used the proximity ligation assay immune detection technique to demonstrate that during entry HPV16 L2 traffics into and out of the early endosome prior to Golgi localization, and we demonstrated that L2 enters the endoplasmic reticulum during entry. The cellular membrane-associated protease, γ-secretase, is required for infection by HPV16 pseudovirus and authentic HPV16. We also showed that inhibition of γ-secretase does not interfere substantively with virus internalization, initiation of capsid disassembly, entry into the early endosome, or exit from this compartment, but γ-secretase is required for localization of L2 and viral DNA to the Golgi apparatus and the endoplasmic reticulum. These results show that incoming HPV16 traffics sequentially from the cell surface to the endosome and then to the Golgi apparatus and the endoplasmic reticulum prior to nuclear entry.

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Section: Discussionmentioning

confidence: 99%

Vesicular Trafficking of Incoming Human Papillomavirus 16 to the Golgi Apparatus and Endoplasmic Reticulum Requires γ-Secretase Activity

Zhang

Kazakov

Popa

et al. 2014

mBio

128

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“…Specifically, dynein promotes the coupling of centrosomes to the NE, has been hypothesized to assist in NEBD, and functions along the mitotic spindle to facilitate chromosome segregation at anaphase (Lippincott-Schwartz, 2002; Dujardin et al. , 2003; Tanenbaum et al.…”

Section: Discussionmentioning

confidence: 99%

Human Asunder promotes dynein recruitment and centrosomal tethering to the nucleus at mitotic entry

Jodoin

Shboul

Sitaram

et al. 2012

MBoC

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“…Studies of the formation of such assemblages will be more demanding. The simulation of more complex cellular activities, such as synaptic transmission718 and the dismantling of the nuclear membrane on cell division by the motor protein cytoplasmic dynein719 are two examples of interest. Much of this work will build on the detailed knowledge of the structure and dynamics of the channels, enzymes and other cellular components.…”

Section: Epilogue: the History And Future Of Charmm (Martin Karmentioning

confidence: 99%

CHARMM: The biomolecular simulation program

et al. 2009

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CHARMM (Chemistry at HARvard Molecular Mechanics) is a highly versatile and widely used molecular simulation program. It has been developed over the last three decades with a primary focus on molecules of biological interest, including proteins, peptides, lipids, nucleic acids, carbohydrates and small molecule ligands, as they occur in solution, crystals, and membrane environments. For the study of such systems, the program provides a large suite of computational tools that include numerous conformational and path sampling methods, free energy estimators, molecular minimization, dynamics, and analysis techniques, and model-building capabilities. In addition, the CHARMM program is applicable to problems involving a much broader class of many-particle systems. Calculations with CHARMM can be performed using a number of different energy functions and models, from mixed quantum mechanical-molecular mechanical force fields, to all-atom classical potential energy functions with explicit solvent and various boundary conditions, to implicit solvent and membrane models. The program has been ported to numerous platforms in both serial and parallel architectures. This paper provides an overview of the program as it exists today with an emphasis on developments since the publication of the original CHARMM paper in 1983.

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Ripping up the nuclear envelope

Cited by 23 publications

References 14 publications

Vesicular Trafficking of Incoming Human Papillomavirus 16 to the Golgi Apparatus and Endoplasmic Reticulum Requires γ-Secretase Activity

Vesicular Trafficking of Incoming Human Papillomavirus 16 to the Golgi Apparatus and Endoplasmic Reticulum Requires γ-Secretase Activity

Human Asunder promotes dynein recruitment and centrosomal tethering to the nucleus at mitotic entry

CHARMM: The biomolecular simulation program

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