Protein transport articles within Nature Communications

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  • Article
    | Open Access

    Import of proteins into peroxisomes depends on PEX5, PEX13 and PEX14. Here the authors obtain crystal structures and NMR data to show the recognition of diaromatic peptide motifs on a noncanonical surface of the PEX13 SH3 domain, revealing a dynamic network which modulates peroxisomal matrix import.

    • Stefan Gaussmann
    • , Rebecca Peschel
    •  & Michael Sattler

  • Article
    | Open Access

    How RNA polymerase II subunits enter the nucleus is not well understood. Here, the authors show that Transport and Golgi organization protein 6, TANGO6, recruits RNA polymerase II subunit B2, RPB2, to the ER membrane in a retrograde manner and transports it to the nucleus with the aid of importins.

    • Zhi Feng
    • , Shengnan Liu
    •  & Li Li

  • Article
    | Open Access

    Protein function depends on their subcellular location and turnover rate. Here, the authors report a method to measure spatial and temporal proteome dynamics simultaneously, revealing compartment-specific protein turnover and translocation in cardiac cells under ER stress and carfilzomib treatment.

    • Jordan Currie
    • , Vyshnavi Manda
    •  & Edward Lau

  • Article
    | Open Access

    Botulinum neurotoxins (BoNTs), the causative agents of the disease botulism, are potent biological toxins. Here the authors use Designed Ankyrin Repeat Proteins (DARPins) to probe BoNT structure and function: DARPin-F5 that completely blocks SNAP25 substrate cleavage by BoNT/A1 in vitro was identified.

    • Oneda Leka
    • , Yufan Wu
    •  & Richard A. Kammerer

  • Article
    | Open Access

    Tail-anchored (TA) membrane protein biogenesis is mediated by the GET insertase. Here, authors present cryo-EM and X-ray structures, MD simulations and functional data for human and fungal insertases showing membrane remodeling for TA insertion.

    • Melanie A. McDowell
    • , Michael Heimes
    •  & Irmgard Sinning

  • Article
    | Open Access

    Intestinal cholesterol is taken into endocytic recycling compartment via NPC1L1-mediated endocytosis. Here the authors show that certain bile acids facilitate cholesterol transport to the endoplasmic reticulum from endocytic recycling compartment in cells and NPC1L1 is then recycled back to the plasma membrane.

    • Jian Xiao
    • , Le-Wei Dong
    •  & Bao-Liang Song

  • Article
    | Open Access

    Selenium and copper are two essential trace elements whose homeostasis and distribution is regulated by hepatic release of selenoprotein P (SELENOP) and ceruloplasmin, respectively. Here, the authors show that excessive copper results in hepatic SELENOP accumulation in the trans Golgi which might limit the selenium transport to peripheral organs.

    • Maria Schwarz
    • , Caroline E. Meyer
    •  & Anna P. Kipp

  • Article
    | Open Access

    The Hedgehog morphogen creates gradients during development, but diffusion alone cannot explain its spatiotemporal dynamics. Hedgehog transport requires binding heparan sulfate sugar chains, and the authors now show that Hedgehogs can spread by interacting with sequential heparan molecules.

    • Fabian Gude
    • , Jurij Froese
    •  & Kay Grobe

  • Article
    | Open Access

    The mitochondrial ATP synthase produces the bulk of cellular ATP. Here, the authors report a function of the mitochondrial Hsp70 in the formation of the catalytical head and in its assembly with the peripheral stalk to form the mature ATP synthase.

    • Jiyao Song
    • , Liesa Steidle
    •  & Thomas Becker

  • Article
    | Open Access

    Microbial DNA is recognized by the cGAS-STING pathway, which leads to a type I interferon response. Here authors show that a basal flux of interferon activation could also be triggered by interference with STING trafficking from the Golgi apparatus to the lysosomes.

    • Xintao Tu
    • , Ting-Ting Chu
    •  & Nan Yan

  • Article
    | Open Access

    Here the authors address how embryos control the timing of specific gene activation in early frog development. They find transcription factors for early gene activation are maternally loaded and remain at constant levels, and rather that order of activation is based on their sequential entry into the nucleus based largely on their respective affinity to importins.

    • Thao Nguyen
    • , Eli J. Costa
    •  & Martin Wühr

  • Article
    | Open Access

    The DEAD box protein DDX1 is known to form large aggregates in the cytoplasm of early mouse embryos. Here the authors identify DDX1-containing vesicles and show that loss of Ddx1 affects their integrity, compromising mitochondria function and causing embryonic lethality.

    • Yixiong Wang
    • , Lubna Yasmin
    •  & Roseline Godbout

  • Article
    | Open Access

    Although ubiquitin ligases are known to control clock protein degradation, their other roles in clock neurons are unclear. Here the authors report that UBR4 promotes export of neuropeptides from the Golgi for axonal trafficking, which is important for circadian clock synchrony in mice and flies.

    • Sara Hegazi
    • , Arthur H. Cheng
    •  & Hai-Ying Mary Cheng

  • Article
    | Open Access

    TDP-43 is a nucleic acid binding protein, whose insoluble aggregates are neuropathological hallmarks of specific subsets of patients with amyotrophic lateral sclerosis and frontotemporal lobar degeneration. Post-translational modifications and acetylation of TDP-43 impact its interaction with RNA, its localization in the cells, and are linked to disease. Using antibodies generated against TDP-43 lysine acetylation sites, sirtuin-1 was found to potently deacetylate amber suppressed [acK136]TDP-43 and reduce its aggregation propensity. Thus, distinct lysine acetylations modulate nuclear import, RNA binding as well as phase separation and aggregation of TDP-43, suggesting regulatory mechanisms for TDP-43 pathogenesis.

    • Jorge Garcia Morato
    • , Friederike Hans
    •  & Philipp J. Kahle

  • Article
    | Open Access

    The translation of mechanical cues into gene expression changes is dependent on the nuclear import of mechanoresponsive transcriptional regulators. Here the authors identify that Importin-7 drives the nuclear import of one such regulator YAP while YAP then controls Importin-7 response to mechanical cues and restricts Importin-7 binding to other cargoes.

    • María García-García
    • , Sara Sánchez-Perales
    •  & Miguel A. Del Pozo

  • Article
    | Open Access

    Microtubule tracks are important for the transport of molecules within axons. Here, the authors show that ATAT1, the enzyme responsible for acetylating a-tubulin, receives acetyl groups from ATP citrate lyase whose stability is regulated by Elongator, a protein mutated in the neuronal disease Familial dysautonomia.

    • Aviel Even
    • , Giovanni Morelli
    •  & Laurent Nguyen

  • Article
    | Open Access

    The TOM and TIM23 complexes facilitate the transport of nuclear-encoded proteins into the mitochondrial matrix. Here, the authors use a stalled client protein to purify the translocation supercomplex and gain insight into the TOM-TIM23 interface and the mechanism of protein handover from the TOM to the TIM23 complex.

    • Ridhima Gomkale
    • , Andreas Linden
    •  & Peter Rehling

  • Article
    | Open Access

    NEK1 mutations promote lethality early in life and ALS late in life via unknown mechanisms. Here, the authors show that NEK1 mutation disrupts retromer-mediated trafficking and promotes RIPK1 activation, connecting retromer trafficking and metabolism to neuroinflammation by dietary intervention.

    • Huibing Wang
    • , Weiwei Qi
    •  & Junying Yuan

  • Article
    | Open Access

    The permeability barrier of nuclear pore complexes blocks passage of inert macromolecules but allows rapid, receptor-mediated, and RanGTPase-driven transport of cargoes up to ribosome size. The authors now show that such a barrier can be faithfully recapitulated by an ultimately simplified FG phase assembled solely from a tandemly repeated 12mer GLFG peptide.

    • Sheung Chun Ng
    • , Thomas Güttler
    •  & Dirk Görlich

  • Article
    | Open Access

    Type-III secretion systems (T3SSs) are capable of translocating proteins with high speed while maintaining the membrane barrier for small molecules. Here, a structure-function analysis of the T3SS pore complex elucidates the precise mechanisms enabling the gating and the conformational changes required for protein substrate secretion.

    • Svenja Hüsing
    • , Manuel Halte
    •  & Thibaud T. Renault

  • Article
    | Open Access

    Bacteria use the type 2 secretion system to secrete enzymes and toxins across the outer membrane to the environment. Here the authors analyse the T2SS pathway in three protist lineages and suggest that the early mitochondrion may have been capable of secreting proteins into the cytosol.

    • Lenka Horváthová
    • , Vojtěch Žárský
    •  & Pavel Doležal

  • Article
    | Open Access

    The mechanisms by which platelets release sphingosine-1-phosphate (S1P) is not well characterized. Here the authors show that Mfsd2b is required for S1P release from both resting and activated platelets and that deletion of Mfsd2b impairs thrombotic functions of platelets.

    • Madhuvanthi Chandrakanthan
    • , Toan Quoc Nguyen
    •  & Long N. Nguyen

  • Article
    | Open Access

    Most mitochondrial proteins are imported from the cytosol and must fold in the mitochondria. Here, the authors show that the mitochondrial protease LONP1 plays a critical role in the mtHSP70 chaperone system independently of its protease activity.

    • Chun-Shik Shin
    • , Shuxia Meng
    •  & David C. Chan

  • Article
    | Open Access

    Biochemistry combined with biophysical measurements and mathematical modeling offer insight into the mechanism by which the cotranslational chaperone, nascent polypeptide-associated complex (NAC), modulates substrate selection by signal recognition particle (SRP) and reduces aberrant, nonspecific targeting of ribosomes to the ER.

    • Hao-Hsuan Hsieh
    • , Jae Ho Lee
    •  & Shu-ou Shan

  • Article
    | Open Access

    The transcriptional regulator YAP shuttles rapidly between the cytoplasm and nucleus, but whether and how dynamics such as amplitude and frequency affect target gene transcription is unclear. Here, using live imaging of endogenous YAP and target-gene transcription, the authors show that YAP-dependent signalling is encoded through rapid and concerted changes in the nucleo-cytoplasmic distribution of YAP.

    • J. Matthew Franklin
    • , Rajarshi P. Ghosh
    •  & Jan T. Liphardt

  • Article
    | Open Access

    The ATPase SecA drives Sec-dependent protein translocation across the bacterial plasma membrane. Here, the authors combine kinetic translocation measurements with single-molecule force spectroscopy and demonstrate that the SecA motor generates mechanical force to unfold and translocate preproteins.

    • Riti Gupta
    • , Dmitri Toptygin
    •  & Christian M. Kaiser

  • Article
    | Open Access

    Import of proteins into specific cellular compartments is critical for organelle function and several proteins are known to be imported into multiple compartments. Here, the authors report that the protein Ptc5 is first sorted to and processed in the mitochondria before being targeted to peroxisomes, which may influence mitochondria-peroxisome interorganellar contact.

    • Thorsten Stehlik
    • , Marco Kremp
    •  & Johannes Freitag

  • Article
    | Open Access

    Most cells possess sensory cilia, which need to be gated properly. Here the authors show that the C. elegans proteins TALP-3 and ANKR-26 coordinate cilia gating in the context of transition fibers and that this mechanism is conserved in mammalian cells and likely implicated in certain ciliopathies.

    • Hao Yan
    • , Chuan Chen
    •  & Qing Wei

  • Article
    | Open Access

    The contribution of central and peripheral channels of nuclear pores to transport of transmembrane proteins is unclear. Here the authors show that most inner nuclear membrane proteins use only peripheral channels, but some extend nuclear localization signals into the central channel for directed nuclear transport.

    • Krishna C. Mudumbi
    • , Rafal Czapiewski
    •  & Weidong Yang

  • Article
    | Open Access

    Proteins are translocated across membranes through the Sec61/SecY channel. Here, the authors present the structure of a translocating peptide chain trapped inside the SecA-SecY complex which suggests how peptides are actively moved through the channel.

    • Chengying Ma
    • , Xiaofei Wu
    •  & Long Li

  • Article
    | Open Access

    Synaptic plasticity ensures functionality during perturbations and enables memory formation. Here, the authors describe homeostatic functional and nano-modular active zone modifications for immediate and long-lasting enhancement of neurotransmitter release, and identify Unc13 as a presynaptic molecular target for homeostatic potentiation and learning.

    • Mathias A. Böhme
    • , Anthony W. McCarthy
    •  & Alexander M. Walter

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