April 2009 Volume 11 Number 4, pp 363 - 508
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Article Series on Post-transcriptional control
Nature Reviews Molecular Cell Biology has launched an Article Series that assesses the
mechanisms of post-transcriptional control, including mRNA processing, splicing,
mRNA localization, translation and noncoding-RNA-medicated mechanisms.
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EDITORIALS
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UK research funding p363
Is the UK still committed to basic biology research?
doi:10.1038/ncb0409-363a
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Turning points p363
A series of essays describing pivotal events in the careers of cell biologists.
doi:10.1038/ncb0409-363b
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TURNING POINTS
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Coming in from the cold: how answering a postcard can launch a
scientific career p364
Gottfried Schatz
doi:10.1038/ncb0409-364
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REVIEW
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Spindle orientation during asymmetric cell division pp365 - 374
Karsten H. Siller and Chris Q. Doe
doi:10.1038/ncb0409-365
Abstract: http://links.ealert.nature.com/ctt?kn=25&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
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NEWS AND VIEWS
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Double JMY: making actin fast pp375 - 376
The assembly of actin networks is dependent on nucleation-promoting
factors. A new study identifies JMY as a protein containing two separate
nucleation-promoting activities that shuttles between the nucleus and the
cytoplasm and promotes cell migration. These observations indicate that
JMY is an important factor controlling actin dynamics in motile cells.
David W. Roadcap and James E. Bear
doi:10.1038/ncb0409-375
http://links.ealert.nature.com/ctt?kn=120&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
Skp2: caught in the Akt pp377 - 379
To control cell proliferation, signal transduction needs to regulate the
cell-cycle machinery. Recent findings show that Akt -- a major
kinase that coordinates diverse signalling pathways -- phosphorylates
Skp2, a subunit of the SCF-Skp2 ubiquitin ligase that targets key
cell-cycle regulators. Akt1-dependent phosphorylation activates
SCF-Skp2 through multiple mechanisms.
Karin Ecker and Ludger Hengst
doi:10.1038/ncb0409-377
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Targeting protein ubiquitylation: DDB1 takes its RING off pp379 - 381
Ubiquitin E3 ligases of the RING and HECT families are distinct not
only in their catalytic mechanisms but also in targeting substrates.
Now it seems that one heterodimeric complex can target substrates
to both types of E3 ligase.
Sarah Jackson and Yue Xiong
doi:10.1038/ncb0409-379
http://links.ealert.nature.com/ctt?kn=86&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
SOC: now also store-operated cyclase pp381 - 382
Depletion of Ca2+ from intracellular stores has long been known to signal
to and activate plasma membrane 'store-operated' channels. We now
learn that store depletion also controls the formation of cyclic AMP (cAMP)
through the regulation of adenylyl cyclase (A-Cyclase). These findings
substantially broaden the scope and biological significance of Ca2+
store-regulated signalling.
James W. Putney, Jr
doi:10.1038/ncb0409-381
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Research highlights p383
doi:10.1038/ncb0409-383
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ARTICLES
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Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate
autophagy at different stages pp385 - 396
Beclin 1 is an essential mediator of mammalian autophagy that has
anti-tumour activity. Beclin 1 associates with Atg14L and Rubicon to
regulate autophagosome formation and maturation, respectively.
Kohichi Matsunaga et al.
doi:10.1038/ncb1846
Abstract: http://links.ealert.nature.com/ctt?kn=4&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
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Phosphorylation by Akt1 promotes cytoplasmic localization of Skp2 and
impairs APCCdh1-mediated Skp2 destruction pp397 - 408
Skp2 is a known component of the SCF ubiquitin ligase that targets the
cell-cycle regulator p27. Akt kinase phosphorylates Skp2 and regulates
its stability and cytoplasmic localization.
Daming Gao et al.
doi:10.1038/ncb1847
Abstract: http://links.ealert.nature.com/ctt?kn=102&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
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Protein kinase DYRK2 is a scaffold that facilitates assembly of an E3 ligase
pp409 - 419
The kinase DYRK2 regulates the assembly of a ubiquitin ligase complex in
a phosphorylation-independent manner, while also phosphorylating the target
for the ligase. Thus, ligase assembly and target ubiquitylation appear to be
physically linked processes.
Subbareddy Maddika and Junjie Chen
doi:10.1038/ncb1848
Abstract: http://links.ealert.nature.com/ctt?kn=19&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
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Phosphorylation-dependent regulation of cytosolic localization and oncogenic
function of Skp2 by Akt/PKB pp420 - 432
Skp2 is a known component of the SCF ubiquitin ligase that ubiquitylates the
cell-cycle regulator p27. Akt kinase directly phosphorylates Skp2 and regulates
SCF complex assembly and ligase activity, Skp2 cytoplasmic localization and
Skp2-dependent regulation of cell proliferation and migration.
Hui-Kuan Lin et al.
doi:10.1038/ncb1849
Abstract: http://links.ealert.nature.com/ctt?kn=74&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=97&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
Store-operated cyclic AMP signalling mediated by STIM1 pp433 - 442
The ER Ca2+ sensor protein STIM1 regulates cAMP signalling by coupling
the changes in luminal ER Ca2+ content to adenylyl cyclase activity.
Konstantinos Lefkimmiatis et al.
doi:10.1038/ncb1850
Abstract: http://links.ealert.nature.com/ctt?kn=64&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=61&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
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LETTERS
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Myosin IIIa boosts elongation of stereocilia by transporting espin 1 to
the plus ends of actin filaments pp443 - 450
Actin filaments in stereocilia on the surface of inner ear sensory hair
cells are continually renewed. Myosin IIIa transports the actin-binding/
bundling protein espin to stereocilia tips and cooperates with espin in
actin filament elongation.
Felipe T. Salles et al.
doi:10.1038/ncb1851
Abstract: http://links.ealert.nature.com/ctt?kn=101&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=36&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
p53-cofactor JMY is a multifunctional actin nucleation factor pp451 - 459
JMY, originally discovered as a binding partner of the p53 co-activator
p300, is an actin-nucleating protein, assembling filaments both by
activation of the Arp2/3 complex and through an Arp2/3-independent
mechanism.
J. Bradley Zuchero et al.
doi:10.1038/ncb1852
Abstract: http://links.ealert.nature.com/ctt?kn=14&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
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Characterization of the interface between normal and transformed
epithelial cells pp460 - 467
How a transformed cell interacts with normal cells remains unclear.
Most RasV12-transformed cells in an epithelial monolayer are extruded
apically in a manner regulated by ROCK, Myosin II and Cdc42, but
some cells invade the basal matrix via a mechanism requiring PI3 kinase.
Catherine Hogan et al.
doi:10.1038/ncb1853
Abstract: http://links.ealert.nature.com/ctt?kn=70&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=65&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
Distinct regulation of autophagic activity by Atg14L and Rubicon
associated with Beclin 1-phosphatidylinositol-3-kinase complex
pp468 - 476
Beclin 1 is an essential mediator of mammalian autophagy that has
anti-tumour activity. Two proteins that interact with Beclin 1 have been
newly identified and their analysis shows that distinct Beclin 1 complexes
regulate autophagosome formation and maturation, respectively.
Yun Zhong et al.
doi:10.1038/ncb1854
Abstract: http://links.ealert.nature.com/ctt?kn=3&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=33&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
A mechanism for chromosome segregation sensing by the NoCut checkpoint
pp477 - 483
In yeast, anaphase defects can trigger activation of the NoCut checkpoint,
resulting in delayed cytokinesis. The Ilp1/aurora kinase localizes to the
spindle midzone and monitors chromatin segregation, thus acting as a
chromatin sensor.
Manuel Mendoza et al.
doi:10.1038/ncb1855
Abstract: http://links.ealert.nature.com/ctt?kn=30&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=29&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
Modularity of MAP kinases allows deformation of their signalling pathways
pp484 - 491
During evolution, MAP kinases repeatedly changed substrate specificities
and interaction partners. Because of their modular design, they can be
experimentally re-designed to achieve rewiring of the signalling network.
Areez Mody, Joan Weiner and Sharad Ramanathan
doi:10.1038/ncb1856
Abstract: http://links.ealert.nature.com/ctt?kn=75&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=125&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
STAT3 inhibition of gluconeogenesis is downregulated by SirT1 pp492 - 500
Yongzhan Nie et al.
doi:10.1038/ncb1857
Abstract: http://links.ealert.nature.com/ctt?kn=52&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=62&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
Absence of nucleolar disruption after impairment of 40S ribosome biogenesis
reveals an rpL11-translation-dependent mechanism of p53 induction pp501 - 508
Depletion of ribosomal protein S6 leads to upregulation of p53 and cell cycle
arrest. Surprisingly, p53 induction is not due to nucleolar disruption and Mdm2
inhibition, but rather the selective translation of a class of mRNAs including
ribosomal protein L11.
Stefano Fumagalli et al.
doi:10.1038/ncb1858
Abstract: http://links.ealert.nature.com/ctt?kn=124&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=8&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
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ERRATUM
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Electrochemical cues regulate assembly of the Frizzled/Dishevelled complex
at the plasma membrane during planar epithelial polarization p508
Matias Simons et al.
doi:10.1038/ncb0409-508
http://links.ealert.nature.com/ctt?kn=83&m=32242963&r=MTc2NDEyMTk0MQS2&b=2&j=NDcwNTY0NjMS1&mt=1&rt=0
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