Cytoplasmic Dynein Regulation by Subunit Heterogeneity and Its Role in Apical Transport

Tai, Andrew W.; Chuang, Jen Zen; Sung, Ching Hwa

doi:10.1083/jcb.153.7.1499

Cited by 114 publications

(123 citation statements)

References 55 publications

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“…Cytoplasmic dynein light chain roadblock isoforms (DYNLRB1 and 2) are capable of forming homo and heterodimers [22]. Cytoplasmic dynein light chain Tctex1 (DYNLT) family, either Tctex1 (DYNLT1) or rp3 (DYNLT3), which share 55% amino acid homology [14], are mutually exclusive in cytoplasmic dynein complexes [23]. Despite their similarities, Tctex1 and rp3 exhibit significant differences in cellular and tissue distributions, as well as in their binding specificities [23][24][25][26][27][28][29][30].…”

Section: Dynein Cofactor: Dynactinmentioning

confidence: 99%

Transport and egress of herpes simplex virus in neurons

Diefenbach

Miranda-Saksena

Douglas

et al. 2007

Reviews in Medical Virology

171

150

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The mechanisms of axonal transport of the alphaherpesviruses, HSV and pseudorabies virus (PrV), in neuronal axons are of fundamental interest, particularly in comparison with other viruses, and offer potential sites for antiviral intervention or development of gene therapy vectors. These herpesviruses are transported rapidly along microtubules (MTs) in the retrograde direction from the axon terminus to the dorsal root ganglion and then anterogradely in the opposite direction. Retrograde transport follows fusion and deenvelopment of the viral capsid at the axonal membrane followed by loss of most of the tegument proteins and then binding of the capsid via one or more viral proteins (VPs) to the retrograde molecular motor dynein. The HSV capsid protein pUL35 has been shown to bind to the dynein light chain Tctex1 but is likely to be accompanied by additional dynein binding of an inner tegument protein. The mechanism of anterograde transport is much more controversial with different processes being claimed for PrV and HSV: separate transport of HSV capsid/tegument and glycoproteins versus PrV transport as an enveloped virion. The controversy has not been resolved despite application, in several laboratories, of confocal microscopy (CFM), realtime fluorescence with viruses dual labelled on capsid and glycoprotein, electron microscopy in situ and immunoelectron microscopy. Different processes for each virus seem counterintuitive although they are the most divergent in the alphaherpesvirus subfamily. Current hypotheses suggest that unenveloped HSV capsids complete assembly in the axonal growth cones and varicosities, whereas with PrV unenveloped capsids are only found travelling in a retrograde direction.

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Section: Dynein Cofactor: Dynactinmentioning

confidence: 99%

Transport and egress of herpes simplex virus in neurons

Diefenbach

Miranda-Saksena

Douglas

et al. 2007

Reviews in Medical Virology

171

150

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“…It is very well established that MT motors of the kinesin or dynein families play key roles in the generation and transcytoplasmic transport of tubular and vesicular transporters destined to the apical PM of Madin-Darby canine kidney (MDCK) cells (Kreitzer et al, 2000;Noda et al, 2001;Tai et al, 2001;Allan et al, 2002;Musch, 2004;Jaulin et al, 2007). By contrast, our knowledge of the specific roles of the actin cytoskeleton in intracellular transport routes remains fragmentary, unlike the situation at the PM, where various mechanisms involving the actin cytoskeleton in endocytic routes have been well documented (Erickson et al, 1996;Allan et al, 2002;Luna et al, 2002;Stamnes, 2002;Carreno et al, 2004;Matas et al, 2004;Bonazzi et al, 2005;Perret et al, 2005;Yarar et al, 2005;Egea et al, 2006;McNiven and Thompson, 2006).…”

Section: Introductionmentioning

confidence: 99%

LIM Kinase 1 and Cofilin Regulate Actin Filament Population Required for Dynamin-dependent Apical Carrier Fission from theTrans-Golgi Network

Salvarezza

Deborde

Schreiner

et al. 2009

MBoC

108

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The functions of the actin cytoskeleton in post-Golgi trafficking are still poorly understood. Here, we report the role of LIM Kinase 1 (LIMK1) and its substrate cofilin in the trafficking of apical and basolateral proteins in Madin-Darby canine kidney cells. Our data indicate that LIMK1 and cofilin organize a specialized population of actin filaments at the Golgi complex that is selectively required for the emergence of an apical cargo route to the plasma membrane (PM). Quantitative pulse-chase live imaging experiments showed that overexpression of kinase-dead LIMK1 (LIMK1-KD), or of LIMK1 small interfering RNA, or of an activated cofilin mutant (cofilin S3A), selectively slowed down the exit from the trans-Golgi network (TGN) of the apical PM marker p75-green fluorescent protein (GFP) but did not interfere with the apical PM marker glycosyl phosphatidylinositol-YFP or the basolateral PM marker neural cell adhesion molecule-GFP. Highresolution live imaging experiments of carrier formation and release by the TGN and analysis of peri-Golgi actin dynamics using photoactivatable GFP suggest a scenario in which TGN-localized LIMK1-cofilin regulate a population of actin filaments required for dynamin-syndapin-cortactin-dependent generation and/or fission of precursors to p75 transporters. INTRODUCTIONThe organization of polarized intracellular trafficking to the plasma membrane (PM) involves a close cooperation between cargo proteins, adaptors and cytoskeletal elements that takes place at major sorting organelles, e.g., the Golgi complex and recycling endosomes (Bonifacino and Traub, 2003;Rodriguez-Boulan et al., 2005). Newly synthesized proteins destined for endosomes, lysosomes, and the basolateral PM of epithelial cells segregate into nascent post-Golgi or postendosomal vesicles via tyrosine, dileucine, or monoleucine sorting signals, clathrin adaptors, and accessory proteins (Bonifacino and Traub, 2003;Rodriguez-Boulan et al., 2005;Deborde et al., 2008).By contrast, proteins destined for the apical PM are sorted into nascent post-Golgi transporters via N-and O-glycans, specialized transmembrane or cytoplasmic domains or glycosyl phosphatidylinositol (GPI)-anchors that interact with lipid domains (rafts), lectins, or microtubule (MT) motors (Scheiffele et al., 1995;Simons and Ikonen, 1997;Yeaman et al., 1997;Delacour et al., 2005Delacour et al., , 2006Rodriguez-Boulan et al., 2005). It is very well established that MT motors of the kinesin or dynein families play key roles in the generation and transcytoplasmic transport of tubular and vesicular transporters destined to the apical PM of Madin-Darby canine kidney (MDCK) cells (Kreitzer et al., 2000;Noda et al., 2001;Tai et al., 2001;Allan et al., 2002;Musch, 2004;Jaulin et al., 2007). By contrast, our knowledge of the specific roles of the actin cytoskeleton in intracellular transport routes remains fragmentary, unlike the situation at the PM, where various mechanisms involving the actin cytoskeleton in endocytic routes have been well documented (Erickson et al., 1...

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“…Cytoplasmic dynein superfamily members control various cell functions and are important for establishing epithelial polarity (Tai et al, 2001). Several different subunits of cytoplasmic dynein can bind to a variety of cargoes (Kamal and Goldstein, 2002;Karcher et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

A Novel Transforming Growth Factor-β Receptor-interacting Protein That Is Also a Light Chain of the Motor Protein Dynein

Tang¹,

Staub²,

Gao

et al. 2002

MBoC

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The phosphorylated, activated cytoplasmic domains of the transforming growth factor-␤ (TGF␤) receptors were used as probes to screen an expression library that was prepared from a highly TGF␤-responsive intestinal epithelial cell line. One of the TGF␤ receptor-interacting proteins isolated was identified to be the mammalian homologue of the LC7 family (mLC7) of dynein light chains (DLCs). This 11-kDa cytoplasmic protein interacts with the TGF␤ receptor complex intracellularly and is phosphorylated on serine residues after ligand-receptor engagement. Forced expression of mLC7-1 induces specific TGF␤ responses, including an activation of Jun N-terminal kinase (JNK), a phosphorylation of c-Jun, and an inhibition of cell growth. Furthermore, TGF␤ induces the recruitment of mLC7-1 to the intermediate chain of dynein. A kinase-deficient form of TGF␤ RII prevents both mLC7-1 phosphorylation and interaction with the dynein intermediate chain (DIC). This is the first demonstration of a link between cytoplasmic dynein and a natural growth inhibitory cytokine. Furthermore, our results suggest that TGF␤ pathway components may use a motor protein light chain as a receptor for the recruitment and transport of specific cargo along microtublules. INTRODUCTIONTransforming growth factor-␤ (TGF␤) is the prototype for the TGF␤ superfamily of highly conserved growth regulatory polypeptides that also includes the activins, inhibins, bone morphogenetic proteins, decapentaplegic (Dpp), nodal, Lefty, and others (Roberts, 1998;Sporn and Vilcek, 2000;Yue and Mulder, 2001). Alterations in the TGF␤ signaling components and pathways have been implicated in a vast array of human pathologies, including cancer (Massague et al., 2000;Sporn and Vilcek, 2000;Derynck et al., 2001).TGF␤ binds to two types of transmembrane serine/threonine kinase receptors (RI and RII) in a heterotetrameric complex, to activate downstream components (Roberts, 1998; Massague et al., 2000;Sporn and Vilcek, 2000;Yue and Mulder, 2001). The Smad family of signaling intermediates plays an important role in mediating TGF␤ responses (Attisano and Wrana, 2000;ten Dijke et al., 2000;Yue and Mulder, 2001). Moreover, TGF␤ has been shown to regulate Ras (Mulder and Morris, 1992;Hartsough et al., 1996;Yue et al., 1998) and several components of the mitogen-activated protein kinase (Mapk) pathways (Hartsough and Mulder, 1995;Frey and Mulder, 1997;Mulder, 2000;Sporn and Vilcek, 2000;Yue and Mulder, 2001). In addition to the Ras/Mapk and Smad pathways, several proteins have been identified based upon their interaction with the TGF␤ receptors (Yue and Mulder, 2001). Furthermore, various Smad-interacting proteins have also been identified, including SARA and Dab2, which interact with both Smads and the TGF␤ receptors (Tsukazaki et al., 1998;Hocevar et al., 2001;Yue and Mulder, 2001).Despite advances in our understanding of the mechanisms by which the Smad and Ras/Mapk cascades mediate some TGF␤ effects, these pathways seem to regulate primarily transcriptional events (Hocevar et al., 1...

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Cytoplasmic Dynein Regulation by Subunit Heterogeneity and Its Role in Apical Transport

Cited by 114 publications

References 55 publications

Transport and egress of herpes simplex virus in neurons

Transport and egress of herpes simplex virus in neurons

LIM Kinase 1 and Cofilin Regulate Actin Filament Population Required for Dynamin-dependent Apical Carrier Fission from theTrans-Golgi Network

A Novel Transforming Growth Factor-β Receptor-interacting Protein That Is Also a Light Chain of the Motor Protein Dynein

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