Table of contents
March 2005, Volume 7 No 3 pp203-321
About the coverNews and Views
Pars and polarity: taking control of Rac - pp205 - 207
Toby W. Hurd & Ben Margolis
doi:10.1038/ncb0305-205
In this issue, two groups have examined the role of the Par proteins in the regulation of small G proteins, in two different models of cell polarity — mammalian epithelia and neuronal axon specification. They concurrently report the intriguing finding that the Par-3/Par-6/aPKC complex can regulate the activation of Rac by interaction with the guanine nucleotide exchanger, Tiam1/STEF. Furthermore, they also demonstrate a hitherto under-appreciated role for the Par-3/Par-6/aPKC complex in the regulation of the actin cytoskeleton.
Full Text - Pars and polarity: taking control of Rac | PDF (169 KB) - Pars and polarity: taking control of Rac
See also: Letter by Chen & Macara | Letter by Nishimura et al.
Cdc48–Ufd2–Rad23: the road less ubiquitinated? - pp207 - 209
Omar A. Bazirgan & Randolph Y. Hampton
doi:10.1038/ncb0305-207
Targeting substrates to the proteasome is generally thought to depend on long polyubiquitin chains that form on the substrate. Recent work has led to the provocative proposal that some substrates may be targeted to the proteasome through smaller chains that contain only four to six ubiquitin molecules.
Full Text - Cdc48–Ufd2–Rad23: the road less ubiquitinated? | PDF (281 KB) - Cdc48–Ufd2–Rad23: the road less ubiquitinated?
An endocytic Prk-ing brake - pp210 - 212
Mara C. Duncan & Gregory S. Payne
doi:10.1038/ncb0305-210
Actin polymerization is intimately associated with endocytosis in yeast and mammalian cells. Mechanisms of actin filament assembly in endocytosis are becoming better understood but less is known about how assembly is terminated. In yeast, phosphorylation of Arp2/3 complex activators provides one mechanism for downregulating endocytic actin assembly.
Full Text - An endocytic Prk-ing brake | PDF (226 KB) - An endocytic Prk-ing brake
See also: Letter by Toshima et al.
Growth factor control of autophagy - p212
Markus Wagner
doi:10.1038/ncb0305-212
Full Text - Growth factor control of autophagy | PDF (127 KB) - Growth factor control of autophagy
Stress and death: breaking up the c-Abl/14-3-3 complex in apoptosis - pp213 - 214
Ann Marie Pendergast
doi:10.1038/ncb0305-213
Nuclear accumulation of the c-Abl tyrosine kinase is associated with a pro-apoptotic response after DNA damage, but the mechanism regulating c-Abl nuclear localization is unclear. DNA damage and other stress signals are now shown to induce phosphorylation of 14-3-3 proteins by the c-Jun amino-terminal kinase, disrupting a c-Abl/14-3-3 cytoplasmic complex, and liberating c-Abl for translocation to the nucleus.
Full Text - Stress and death: breaking up the c-Abl/14-3-3 complex in apoptosis | PDF (166 KB) - Stress and death: breaking up the c-Abl/14-3-3 complex in apoptosis
See also: Letter by Yoshida et al.
The Myc trilogy: lord of RNA polymerases - pp215 - 217
Thordur Oskarsson & Andreas Trumpp
doi:10.1038/ncb0305-215
Cancer cells have a raised cellular metabolism, including increased protein biosynthesis. Three new studies now show that the oncoprotein Myc, known to drive cell division, also enhances ribosomal RNA synthesis by RNA polymerase I in addition to controlling RNA polymerase II- and III-regulated gene transcription. This suggests that Myc promotes the generation of crucial components of a functional ribosome.
Full Text - The Myc trilogy: lord of RNA polymerases | PDF (237 KB) - The Myc trilogy: lord of RNA polymerases
See also: Letter by Grewal et al. | Letter by Grandori et al. | Letter by Arabi et al.
Nucleolar targeting runs on GTP cycles - p217
Sowmya Swaminathan
doi:10.1038/ncb0305-217
Full Text - Nucleolar targeting runs on GTP cycles | PDF (125 KB) - Nucleolar targeting runs on GTP cycles
Perspective
Spindle assembly: asters part their separate ways - pp219 - 222
Jody Rosenblatt
doi:10.1038/ncb0305-219
Abstract - | Full Text - Spindle assembly: asters part their separate ways | PDF (535 KB) - Spindle assembly: asters part their separate ways
Book Review
A new tome for the centrosome - p223
Kevin O'Connell reviews Centrosomes in Development and Disease by Erich Nigg
doi:10.1038/ncb0305-223
Full Text - A new tome for the centrosome | PDF (111 KB) - A new tome for the centrosome
Articles
Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 protein is critical for Golgi secretory function - pp225 - 234
Vladimir Litvak, Nili Dahan, Sreekumar Ramachandran, Helena Sabanay & Sima Lev
doi:10.1038/ncb1221
Abstract - | Full Text - Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 protein is critical for Golgi secretory function | PDF (969 KB) - Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 protein is critical for Golgi secretory function | Supplementary information
Functionally distinct kinesin-13 family members cooperate to regulate microtubule dynamics during interphase - pp235 - 245
Vito Mennella, Gregory C. Rogers, Stephen L. Rogers, Daniel W. Buster, Ronald D. Vale & David J. Sharp
doi:10.1038/ncb1222
Abstract - | Full Text - Functionally distinct kinesin-13 family members cooperate to regulate microtubule dynamics during interphase | PDF (2,169 KB) - Functionally distinct kinesin-13 family members cooperate to regulate microtubule dynamics during interphase | Supplementary information
Letters
Phosphoregulation of Arp2/3-dependent actin assembly during receptor-mediated endocytosis - pp246 - 254
Jiro Toshima, Junko Y. Toshima, Adam C. Martin & David G. Drubin
doi:10.1038/ncb1229
First Paragraph - | Full Text - Phosphoregulation of Arp2/3-dependent actin assembly during receptor-mediated endocytosis | PDF (2,222 KB) - Phosphoregulation of Arp2/3-dependent actin assembly during receptor-mediated endocytosis | Supplementary information
See also: News and Views by Duncan & Payne
Cdc42–MRCK and Rho–ROCK signalling cooperate in myosin phosphorylation and cell invasion - pp255 - 261
Simon Wilkinson, Hugh F. Paterson & Christopher J. Marshall
doi:10.1038/ncb1230
First Paragraph - | Full Text - Cdc42–MRCK and Rho–ROCK signalling cooperate in myosin phosphorylation and cell invasion | PDF (633 KB) - Cdc42–MRCK and Rho–ROCK signalling cooperate in myosin phosphorylation and cell invasion | Supplementary information
Par-3 controls tight junction assembly through the Rac exchange factor Tiam1 - pp262 - 269
Xinyu Chen & Ian G. Macara
doi:10.1038/ncb1226
First Paragraph - | Full Text - Par-3 controls tight junction assembly through the Rac exchange factor Tiam1 | PDF (1,961 KB) - Par-3 controls tight junction assembly through the Rac exchange factor Tiam1 | Supplementary information
See also: News and Views by Hurd & Margolis
PAR-6–PAR-3 mediates Cdc42-induced Rac activation through the Rac GEFs STEF/Tiam1 - pp270 - 277
Takashi Nishimura, Tomoya Yamaguchi, Katsuhiro Kato, Masato Yoshizawa, Yo-ichi Nabeshima, Shigeo Ohno, Mikio Hoshino & Kozo Kaibuchi
doi:10.1038/ncb1227
First Paragraph - | Full Text - PAR-6–PAR-3 mediates Cdc42-induced Rac activation through the Rac GEFs STEF/Tiam1 | PDF (2,028 KB) - PAR-6–PAR-3 mediates Cdc42-induced Rac activation through the Rac GEFs STEF/Tiam1 | Supplementary information
See also: News and Views by Hurd & Margolis
JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-Abl in the apoptotic response to DNA damage - pp278 - 285
Kiyotsugu Yoshida, Tomoko Yamaguchi, Tohru Natsume, Donald Kufe & Yoshio Miki
doi:10.1038/ncb1228
First Paragraph - | Full Text - JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-Abl in the apoptotic response to DNA damage | PDF (536 KB) - JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-Abl in the apoptotic response to DNA damage | Supplementary information
See also: News and Views by Pendergast
Atrophy of S6K1-/- skeletal muscle cells reveals distinct mTOR effectors for cell cycle and size control - pp286 - 294
Mickaël Ohanna, Andrew K. Sobering, Thomas Lapointe, Lazaro Lorenzo, Christophe Praud, Emmanuel Petroulakis, Nahum Sonenberg, Paul A. Kelly, Athanassia Sotiropoulos & Mario Pende
doi:10.1038/ncb1231
First Paragraph - | Full Text - Atrophy of S6K1-/- skeletal muscle cells reveals distinct mTOR effectors for cell cycle and size control | PDF (960 KB) - Atrophy of S6K1-/- skeletal muscle cells reveals distinct mTOR effectors for cell cycle and size control | Supplementary information
Myc-dependent regulation of ribosomal RNA synthesis during Drosophila development - pp295 - 302
Savraj S. Grewal, Ling Li, Amir Orian, Robert N. Eisenman & Bruce A. Edgar
doi:10.1038/ncb1223
First Paragraph - | Full Text - Myc-dependent regulation of ribosomal RNA synthesis during Drosophila development | PDF (1,585 KB) - Myc-dependent regulation of ribosomal RNA synthesis during Drosophila development | Supplementary information
See also: News and Views by Oskarsson & Trumpp
c-Myc associates with ribosomal DNA and activates RNA polymerase I transcription - pp303 - 310
Azadeh Arabi, Siqin Wu, Karin Ridderstråle, Holger Bierhoff, Chiounan Shiue, Karoly Fatyol, Sara Fahlén, Per Hydbring, Ola Söderberg, Ingrid Grummt, Lars-Gunnar Larsson & Anthony P. H. Wright
doi:10.1038/ncb1225
First Paragraph - | Full Text - c-Myc associates with ribosomal DNA and activates RNA polymerase I transcription | PDF (609 KB) - c-Myc associates with ribosomal DNA and activates RNA polymerase I transcription
See also: News and Views by Oskarsson & Trumpp
c-Myc binds to human ribosomal DNA and stimulates transcription of rRNA genes by RNA polymerase I - pp311 - 318
Carla Grandori, Natividad Gomez-Roman, Zoe A. Felton-Edkins, Celine Ngouenet, Denise A. Galloway, Robert N. Eisenman & Robert J. White
doi:10.1038/ncb1224
First Paragraph - | Full Text - c-Myc binds to human ribosomal DNA and stimulates transcription of rRNA genes by RNA polymerase I | PDF (961 KB) - c-Myc binds to human ribosomal DNA and stimulates transcription of rRNA genes by RNA polymerase I | Supplementary information
See also: News and Views by Oskarsson & Trumpp
Brief Communication
Imaging of single light-responsive clock cells reveals fluctuating free-running periods - pp319 - 321
Amanda-Jayne F. Carr & David Whitmore
doi:10.1038/ncb1232
Abstract - | Full Text - Imaging of single light-responsive clock cells reveals fluctuating free-running periods | PDF (549 KB) - Imaging of single light-responsive clock cells reveals fluctuating free-running periods | Supplementary information


