Molecular Biology of the Cell (MOL BIOL CELL)

Publisher: American Society for Cell Biology, American Society for Cell Biology

Journal description

Molecular Biology of the Cell, the journal owned and published by The American Society for Cell Biology, publishes papers that describe and interpret results of original research concerning the molecular aspects of cell structure and function. Studies whose scope bridges several areas of biology are particularly encouraged, for example cell biology and genetics. The aim of the Journal is to publish papers describing substantial research progress in full: papers should include all previously unpublished data and methods essential to support the conclusions drawn.

Current impact factor: 4.47

Impact Factor Rankings

2016 Impact Factor Available summer 2017
2014 / 2015 Impact Factor 4.466
2013 Impact Factor 4.548
2012 Impact Factor 4.604
2011 Impact Factor 4.942
2010 Impact Factor 5.861
2009 Impact Factor 5.979
2008 Impact Factor 5.558
2006 Impact Factor 6.562
2005 Impact Factor 6.52
2004 Impact Factor 7.517
2003 Impact Factor 7.454
2002 Impact Factor 7.599
2001 Impact Factor 7.7
2000 Impact Factor 8.482
1999 Impact Factor 7.527
1998 Impact Factor 8.256
1997 Impact Factor 8.926
1996 Impact Factor 9.915
1995 Impact Factor 9.376
1994 Impact Factor 10.051
1993 Impact Factor 9.025

Impact factor over time

Impact factor
Year

Additional details

5-year impact 4.81
Cited half-life 8.40
Immediacy index 0.86
Eigenfactor 0.07
Article influence 2.19
Website Molecular Biology of the Cell website
Other titles Molecular biology of the cell, MBC
ISSN 1059-1524
OCLC 24486692
Material type Periodical, Internet resource
Document type Journal / Magazine / Newspaper, Internet Resource

Publisher details

American Society for Cell Biology

  • Pre-print
    • Author cannot archive a pre-print version
  • Post-print
    • Author cannot archive a post-print version
  • Conditions
    • On author's personal website or institutional repository
    • Publisher's version/PDF must be used
    • In Press version must not be used
    • Publisher copyright and source must be acknowledged with citation
    • Must link to publisher version
    • Creative Commons Attribution Non-Commercial Share Alike 3.0 License
    • Articles are placed in PubMed Central after 2 months by publisher
  • Classification
    blue

Publications in this journal

  • K. Ono · S. Ono

    No preview · Article · Feb 2016 · Molecular Biology of the Cell
  • J. Konen · S. Wilkinson · B. Lee · H. Fu · W. Zhou · Y. Jiang · A. I. Marcus

    No preview · Article · Feb 2016 · Molecular Biology of the Cell
  • D. J. Omnus · A. G. Manford · J. M. Bader · S. D. Emr · C. J. Stefan

    No preview · Article · Feb 2016 · Molecular Biology of the Cell
  • T. K. Fujiwara · K. Iwasawa · Z. Kalay · T. A. Tsunoyama · Y. Watanabe · Y. M. Umemura · H. Murakoshi · K. G. N. Suzuki · Y. L. Nemoto · N. Morone · A. Kusumi

    No preview · Article · Feb 2016 · Molecular Biology of the Cell
  • T. Oda · T. Abe · H. Yanagisawa · M. Kikkawa

    No preview · Article · Feb 2016 · Molecular Biology of the Cell
  • D. E. Saslowsky · J. R. Thiagarajah · B. A. McCormick · J. C. Lee · W. I. Lencer

    No preview · Article · Feb 2016 · Molecular Biology of the Cell
  • P. Cekan · K. Hasegawa · Y. Pan · E. Tubman · D. Odde · J.-Q. Chen · M. A. Herrmann · S. Kumar · P. Kalab

    No preview · Article · Feb 2016 · Molecular Biology of the Cell
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    ABSTRACT: Clathrin is a ubiquitous protein that mediates membrane traffic at many locations. To function, clathrin requires clathrin adaptors that link it to transmembrane protein cargo. In addition to this cargo selection function, many adaptors also play mechanistic roles in the formation of the transport carrier. However, the full spectrum of these mechanistic roles is poorly understood. Here we report that Ent5, an endosomal clathrin adaptor in Saccharomyces cerevisiae, regulates the behavior of clathrin coats after the recruitment of clathrin. We show that loss of Ent5 disrupts clathrin dependent traffic and prolongs the lifespan of endosomal structures that contain clathrin and other adaptors, suggesting a defect in coat maturation at a late stage. We find that the direct binding of Ent5 with clathrin is required for its role in coat behavior and cargo traffic. Surprisingly, the interaction of Ent5 with other adaptors is dispensable for coat behavior, but not cargo traffic. These findings support a model in which Ent5 clathrin binding performs a mechanistic role in coat maturation, whereas Ent5 adaptor binding promotes cargo incorporation.
    No preview · Article · Feb 2016 · Molecular Biology of the Cell

  • No preview · Article · Feb 2016 · Molecular Biology of the Cell
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    ABSTRACT: Mechanical force-induced cytoskeletal reorganization is essential for cell and tissue remodeling and homeostasis; however, the underlying cellular mechanisms remain elusive. Solo (ARHGEF40) is a RhoA-targeting guanine nucleotide exchange factor (GEF) involved in cyclical stretch-induced human endothelial cell reorientation and convergent extension cell movement in zebrafish gastrula. In this study, we show that Solo binds to keratin-8/keratin-18 (K8/K18) intermediate filaments through multiple sites. Solo overexpression promoted the formation of thick actin stress fibers and keratin bundles, whereas knockdown of Solo, expression of a GEF-inactive mutant of Solo, or inhibition of ROCK suppressed stress fiber formation and led to disorganized keratin networks, indicating that the Solo-RhoA-ROCK pathway serves to precisely organize keratin networks as well as to promote stress fibers. Importantly, knockdown of Solo or K18 or overexpression of GEF-inactive or deletion mutants of Solo suppressed tensile force-induced stress fiber reinforcement. Furthermore, knockdown of Solo or K18 suppressed tensile force-induced RhoA activation. These results strongly suggest that the interplay between Solo and K8/K18 filaments plays a crucial role in tensile force-induced RhoA activation and consequent actin cytoskeletal reinforcement.
    Preview · Article · Jan 2016 · Molecular Biology of the Cell
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    ABSTRACT: Small G-proteins are key regulatory molecules that activate the actin nucleation machinery to drive cytoskeletal rearrangements during plasma membrane remodeling. However, the ability of small G-proteins to interact with nucleation factors on internal membranes to control trafficking processes has not been well characterized. Here, we investigated roles for members of the Rho, Arf, and Rab G-protein families in regulating WHAMM (WASP Homolog associated with Actin, Membranes, and Microtubules), an activator of Arp2/3 complex-mediated actin nucleation. We found that Rab1 stimulated the formation and elongation of WHAMM-associated membrane tubules in cells. Active Rab1 recruited WHAMM to dynamic tubulo-vesicular structures in fibroblasts, and an active prenylated version of Rab1 bound directly to an N-terminal domain of WHAMM in vitro. In contrast to other G-protein-nucleation factor interactions, Rab1 binding inhibited WHAMM-mediated actin assembly. This ability of Rab1 to regulate WHAMM and the Arp2/3 complex represents a distinct strategy for membrane remodeling in which a Rab G-protein recruits the actin nucleation machinery but dampens its activity.
    Preview · Article · Jan 2016 · Molecular Biology of the Cell
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    ABSTRACT: Drosophila Nedd4 (dNedd4) is a HECT ubiquitin ligase with two main splice isoforms: dNedd4 short (dNedd4S) and long (dNedd4Lo). DNedd4Lo has a unique N-terminus containing a Pro-rich region. We previously showed that while dNedd4S promotes neuromuscular synaptogenesis, dNedd4Lo inhibits it and impairs larval locomotion. To delineate the cause of the impaired locomotion, we searched for binding partners to the N-terminal unique region of dNedd4Lo in larval lysates using mass-spectrometry and identified Amphiphysin (dAmph). dAmph is a postsynaptic protein containing SH3-BAR domains, which regulates muscle transverse tubule (T-tubule) formation in flies. We validated the interaction by coimmunoprecipitation and showed direct binding between dAmph-SH3 domain and dNedd4Lo-N-terminus. Accordingly, dNedd4Lo was colocalized with dAmph postsynaptically and at muscle T-tubules. Moreover, expression of dNedd4Lo in muscle during embryonic development led to disappearance of dAmph and to impaired T-tubule formation, phenocopying amph null mutants. This effect was not seen in muscles expressing dNedd4S or a catalytically-inactive dNedd4Lo(C->A). We propose that dNedd4Lo destabilizes dAmph in muscles, leading to impaired T-tubule formation and muscle function.
    Preview · Article · Jan 2016 · Molecular Biology of the Cell
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    ABSTRACT: Phosphatidylinositol 4-kinase IIα (PtdIns4KIIα) localizes to the trans-Golgi network and endosomal compartments and has been implicated in the regulation of endosomal traffic, but the role of both its enzymatic activity and the site of its action have not been elucidated. This study shows that PtdIns4KIIα is required for production of endosomal phosphatidylinositol 4-phosphate (PtdIns(4)P) on early endosomes and for the sorting of transferrin and epidermal growth factor receptor into recycling and degradative pathways. Depletion of PtdIns4KIIα with siRNA significantly reduced the amount of vesicular PtdIns(4)P on early endosomes but not on Golgi membranes. Cells depleted of PtdIns4KIIα had an impaired ability to sort molecules destined for recycling from early endosomes. We further identify the Eps15 homology domain-containing protein EHD3 as a possible endosomal effector of PtdIns4KIIα. Tubular endosomes containing EHD3 were shortened and became more vesicular in PtdIns4KIIα-depleted cells. Endosomal PtdIns(4,5)P2 was also significantly reduced in PtdIns4KIIα-depleted cells. These results show that PtdIns4KIIα regulates receptor sorting at early endosomes through a PtdIns(4)P-dependent pathway and contributes substrate for the synthesis of endosomal PtdIns(4,5)P2.
    No preview · Article · Jan 2016 · Molecular Biology of the Cell
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    ABSTRACT: Intracellular transport involves the regulation of microtubule motor interactions with cargo, but the underlying mechanisms are not well understood. Septins are membrane- and microtubule-binding proteins that assemble into filamentous, scaffold-like structures. Septins are implicated in microtubule-dependent transport, but their roles are unknown. Here, we have uncovered a novel interaction between KIF17, a kinesin 2 family motor, and septin 9 (SEPT9). We show that SEPT9 associates directly with the C-terminal tail of KIF17, and interacts preferentially with the extended cargo-binding conformation of KIF17. In developing rat hippocampal neurons, SEPT9 partially colocalizes and co-migrates with KIF17. We show that SEPT9 interacts with the KIF17 tail domain that associates with mLin-10/Mint1, a cargo adaptor/scaffold protein, which underlies the mechanism of KIF17 binding to the NMDA receptor subunit 2B (NR2B). Significantly, SEPT9 interferes with binding of the PDZ1 domain of mLin-10/Mint1 to KIF17, and thereby, down-regulates NR2B transport into the dendrites of hippocampal neurons. Measurements of KIF17 motility in live neurons show that SEPT9 does not affect the microtubule-dependent motility of KIF17. These results provide the first evidence of an interaction between septins and a non-mitotic kinesin, and suggest that SEPT9 modulates the interactions of KIF17 with membrane cargo.
    Preview · Article · Jan 2016 · Molecular Biology of the Cell
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    ABSTRACT: While genetic perturbation has been the conventional route to probing bacterial systems, small molecules are showing great promise as probes for cellular complexity. Indeed, systematic investigations of chemical-gene interactions can provide new insights into cell networks and are often starting points for understanding the mechanism of action of novel chemical probes. We have developed a robust and sensitive platform for chemical-genomic investigations in bacteria. The approach monitors colony volume kinetically using transmissive scanning measurements, enabling acquisition of growth rates as well as conventional endpoint measurements. We found that chemical genomic profiles were highly sensitive to concentration, necessitating careful selection of compound concentrations. Roughly 20,000,000 data points were collected for 15 different antibiotics. While 1052 chemical-genetic interactions were identified using the conventional endpoint biomass approach, adding interactions in growth rate resulted in 1564 interactions; a 50-200% increase depending on the drug, with many genes uncharacterized or poorly annotated. The chemical-genetic interaction maps generated from this data reveal common genes likely involved in multidrug resistance. Additionally, the maps identified deletion backgrounds exhibiting class-specific potentiation, revealing conceivable targets for combination approaches to drug discovery. This open platform is highly amenable to kinetic screening of any arrayable strain collection, be it prokaryotic or eukaryotic.
    Preview · Article · Jan 2016 · Molecular Biology of the Cell
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    ABSTRACT: Angiogenesis involves the coordinated growth and migration of endothelial cells (EC) toward a proangiogenic signal. The Wnt Planar Cell Polarity (PCP) pathway, through the recruitment of Dishevelled (Dvl) and Dvl associated activator of morphogenesis (Daam1), has been proposed to regulate cell actin cytoskeleton and microtubule (MT) reorganization for oriented cell migration. Here, we report that Kif26b, a kinesin, and Daam1 cooperatively regulate initiation of EC sprouting and directional migration via MT reorganization. First, we found that Kif26b is recruited within the Dvl3/Daam1 complex. Using a 3D in vitro angiogenesis assay, we showed that Kif26b and Daam1 depletion impairs tip cell polarization and destabilizes extended vascular processes. Kif26b depletion specifically alters EC directional migration and mislocalized MT-Organizing Center (MTOC)/Golgi and Myosin IIB cell rear enrichment, therefore the cell fails to establish a proper front-rear polarity. Interestingly, Kif26b ectopic expression rescues the siDaam1 polarization defect phenotype. Finally, we highlighted that Kif26b functions on MT stabilization, which is indispensable for asymmetrical cell structure reorganization. These data demonstrate that Kif26b together with Dvl3/Daam1 initiates cell polarity through the control of PCP signaling pathway-dependent activation.
    Preview · Article · Jan 2016 · Molecular Biology of the Cell
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    ABSTRACT: Stem cell division is tightly controlled via secreted signaling factors and cell adhesion molecules provided from local niche structures. Molecular mechanisms by which each niche component regulates stem cell behaviors remain to be elucidated. Here we show that heparan sulfate (HS), a class of glycosaminoglycan chains, regulates the number and asymmetric division of germline stem cells (GSCs) in the Drosophila testis. We found that GSC number is sensitive to the levels of 6-O sulfate groups on HS. Loss of 6-O sulfation also disrupted normal positioning of centrosomes, a process required for asymmetric division of GSCs. Blocking HS sulfation specifically in the hub led to increased GSC numbers and mispositioning of centrosomes. The same treatment also perturbed the enrichment of Apc2, a component of the centrosome anchoring machinery, at the hub-GSC interface. This perturbation of the centrosome anchoring process ultimately led to an increase in the rate of spindle misorientation and symmetric GSC division. Our study shows that specific HS modifications provide a novel regulatory mechanism for stem cell asymmetric division. Our results also suggest that HS-mediated niche signaling acts upstream of GSC division orientation control.
    Preview · Article · Jan 2016 · Molecular Biology of the Cell
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    ABSTRACT: C2-domains are widespread motifs that often serve as Ca(2+)-binding modules; some proteins have more than one copy. An open issue is whether these domains, when duplicated within the same parent protein, interact with one-another to regulate function. In the present study, we address the functional significance of interfacial residues between the tandem C2-domains of synaptotagmin (syt)-1, a Ca(2+) sensor for neuronal exocytosis. Substitution of four residues: YHRD, at the domain interface, disrupted the interaction between the tandem C2-domains, altered the intrinsic affinity of syt-1 for Ca(2+), and shifted the Ca(2+)-dependency for binding to membranes and driving membrane fusion in vitro. When expressed in syt-1 KO neurons, the YHRD mutant yielded reductions, as compared with the wild-type protein, in synaptic transmission. These results indicate that physical interactions between the tandem C2-domains of syt-1 contribute to excitation-secretion coupling.
    Preview · Article · Jan 2016 · Molecular Biology of the Cell