16 January, 2009
Volume 33, Issue 1
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Volume 33, Issue 1
On the cover: The image shows a confocal section through a yeast cell expressing Tgl4-GFP (in green) that localizes on the surface of lipid droplets (visualized by staining with Nile red). Tgl4 is a major yeast triacylglycerol lipase that is activated by phosphorylation by cyclin-dependent kinase. Lipolysis-derived metabolites are required to facilitate G1/S transition of the yeast cell cycle. For details, see Kurat et al. (p. 53).
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- Table of Contents
- In This Issue
- Featured Article
- Featured Review
- Featured Topic
- Molecular Mechanisms
@ Cell Press
Most Read Papers
- These are the Top 20 Papers by download from the Molecular Cell web site for the last 30 days.
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The rotating structure of the complex of Seh1 and Nup85 solved by Debler et al. in the December 26 issue. This complex, along with a complex of Sec13 and Nup145C, is proposed to assemble into a repetitive "fence-like" coat around the nuclear pore that shares properties with the COPII coats of vesicles in the secretory pathway.
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Molecular Mechanisms @ Cell Press
- Trends in Biochemical Sciences
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Manfred Schmid and Torben Heick Jensen
- Trends in Genetics
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Eddo Kim, Amir Goren, and Gil Ast
- Trends in Genetics
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Michael Hiller and Matthias Platzer
- Trends in Neurosciences
- John S. Mattick and Mark F. Mehler
Volume 33 Issue 1: January 15, 2008
*FREE REVIEW*
Tobias M. Franks and Jens Lykke-Andersen *FREE REVIEW*
Duncan J. Smith, Charles C. Query, and Maria M. Konarska *FREE TiBS REVIEW*
Nicholas J. McGlincy and Christopher W.J. Smith Gwendolyn M. Wilmes, Megan Bergkessel, Sourav Bandyopadhyay, Michael Shales, Hannes Braberg, Gerard Cagney, Sean R. Collins, Gregg B. Whitworth, Tracy L. Kress, Jonathan S. Weissman, et al. Sara Ann Johnson, Gabrielle Cubberley, and David L. Bentley Cyril Saguez, Manfred Schmid, Jens Raabjerg Olesen, Mohamed Abd El-Hady Ghazy, Xiangping Qu, Mathias Bach Poulsen, Tommy Nasser, Claire Moore, and Torben Heick Jensen Inha Heo, Chirlmin Joo, Jun Cho, Minju Ha, Jinju Han, and V. Narry Kim Christine Ender, Azra Krek, Marc R. Friedländer, Michaela Beitzinger, Lasse Weinmann, Wei Chen, Sébastien Pfeffer, Nikolaus Rajewsky, and Gunter Meister Beate Schwer Sophie Bonnal, Concepción Martínez, Patrik Förch, Angela Bachi, Matthias Wilm, and Juan Valcárcel James Weng, Inna Aphasizheva, Ronald D. Etheridge, Lan Huang, Xiaorong Wang, Arnold M. Falick, and Ruslan Aphasizhev Shakir Sayani, Michael Janis, Chrissie Young Lee, Isabelle Toesca, and Guillaume F. Chanfreau Hanae Sato, Nao Hosoda, and Lynne E. Maquat
For additional reviews on this topic, please see Molecular Mechanisms @ Cell Press.
Current Issue
Volume 33 Issue 1: January 15, 2008
Next issue: January 29, 2009
Included in this issue:
PKC phosphorylation of TRAF2 in TNFα-induced NF-κB signaling
PNRC2 links nonsense-mediated decay to decapping
Suppression of HIV-1 Nef translation by a Sam68 mutant
Trafficking of bacterial transcription regulators
β-TrCP and RSK 1/2-mediated BimEL degradation inhibits apoptosis
MRN and Ctp1 in topoisomerase release from DNA
PNRC2 links nonsense-mediated decay to decapping
Suppression of HIV-1 Nef translation by a Sam68 mutant
Trafficking of bacterial transcription regulators
β-TrCP and RSK 1/2-mediated BimEL degradation inhibits apoptosis
MRN and Ctp1 in topoisomerase release from DNA
Click here for the complete Table of Contents.
Featured Articles
The Featured Articles are freely available to all readers
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Using a systems approach that combines genetic and biochemical analyses, Makhnevych et al. link the SUMO system to a broad range of biological processes, providing a useful resource for the SUMO field. |
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Bax is a key regulator of apoptosis. Fu et al. report that Baxβ is a primate-specific isoform that encodes a proapoptotic protein regulated by a mechanism distinct from the well-studied Baxα protein. Moreover, Baxβ synergizes with Baxα to promote apoptosis. |
Featured Review
The Featured Review is freely available to all readers
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Protein Arginine Methylation in Mammals: Who, What, and Why Mark Bedford and Steven Clark Posttranslational modifications can affect nearly all facets of cellular signaling pathways. The PRMT family of enzymes, together with their binding partners, directs protein arginine methylation. In this Review, Mark Bedford and Steven Clark provide an update on the regulatory mechanisms and cellular effects of arginine methylation in mammals. |
Featured Topic
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RNA processing is often essential for converting primary transcripts to mature, functional RNAs. It regulates RNA biogenesis, stability, and translation efficiency and contributes to the potential diversity of a genome through alternative splicing and RNA editing. The following selection of reviews and articles highlight the diversity of RNA-processing mechanisms and the functional impact of RNA-processing events. |
Tobias M. Franks and Jens Lykke-Andersen *FREE REVIEW*
Duncan J. Smith, Charles C. Query, and Maria M. Konarska *FREE TiBS REVIEW*
Nicholas J. McGlincy and Christopher W.J. Smith Gwendolyn M. Wilmes, Megan Bergkessel, Sourav Bandyopadhyay, Michael Shales, Hannes Braberg, Gerard Cagney, Sean R. Collins, Gregg B. Whitworth, Tracy L. Kress, Jonathan S. Weissman, et al. Sara Ann Johnson, Gabrielle Cubberley, and David L. Bentley Cyril Saguez, Manfred Schmid, Jens Raabjerg Olesen, Mohamed Abd El-Hady Ghazy, Xiangping Qu, Mathias Bach Poulsen, Tommy Nasser, Claire Moore, and Torben Heick Jensen Inha Heo, Chirlmin Joo, Jun Cho, Minju Ha, Jinju Han, and V. Narry Kim Christine Ender, Azra Krek, Marc R. Friedländer, Michaela Beitzinger, Lasse Weinmann, Wei Chen, Sébastien Pfeffer, Nikolaus Rajewsky, and Gunter Meister Beate Schwer Sophie Bonnal, Concepción Martínez, Patrik Förch, Angela Bachi, Matthias Wilm, and Juan Valcárcel James Weng, Inna Aphasizheva, Ronald D. Etheridge, Lan Huang, Xiaorong Wang, Arnold M. Falick, and Ruslan Aphasizhev Shakir Sayani, Michael Janis, Chrissie Young Lee, Isabelle Toesca, and Guillaume F. Chanfreau Hanae Sato, Nao Hosoda, and Lynne E. Maquat
For additional reviews on this topic, please see Molecular Mechanisms @ Cell Press.
