Rhodopsin’s Carboxy-Terminal Cytoplasmic Tail Acts as a Membrane Receptor for Cytoplasmic Dynein by Binding to the Dynein Light Chain Tctex-1

Tai, Andrew W.; Chuang, Jen Zen; Bode, Christian; Wolfrum, Uwe; Sung, Ching Hwa

doi:10.1016/s0092-8674(00)80800-4

Cited by 455 publications

(440 citation statements)

References 58 publications

(9 reference statements)

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“…However, not all apical PM proteins associate with lipid rafts; for example, the apical PM protein 75 neurotrophin receptor (p75) uses O-glycans as its apical sorting signal (Yeaman et al, 1997) through clustering by the lectin galectin 3 (Delacour et al, 2006(Delacour et al, , 2007. Yet a fourth apical sorting mechanism, also lipid raft-independent, is that of rhodopsin, which binds to the microtubule (MT) motor dynein by cytoplasmic determinants as an apical sorting strategy (Tai et al, 1999). MT motors of the kinesin type are also used by other apical proteins for apical targeting, for example, p75, which requires the plus end kinesin 5B for its apical delivery (Jaulin et al, 2007) and influenza hemagglutinin and Annexin XIIIb, which require the minus end kinesin KIFC3 (Noda et al, 2001).…”

Section: Polarized Trafficking Machinerymentioning

confidence: 99%

“…The repositioning of the MTOC to a supranuclear position is also likely dependent on the activity of Par1 (Cohen et al, 2004) and might be mediated by dynein, as in migrating cells (Etienne-Manneville and Hall, 2003). The dual arrangement of MT in polarized MDCK cells accounts for the involvement of both dynein and kinesins in apical transport (Hirokawa, 1998;Tai et al, 1999;Jaulin et al, 2007). Disruption of MT with nocodazole or colchicine disrupts selectively the localization of apical PM proteins (van Zeijl and Matlin, 1990;.…”

Section: Polarized Trafficking Machinerymentioning

confidence: 99%

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The epithelial polarity program: machineries involved and their hijacking by cancer

2008

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The Epithelial Polarity Program (EPP) adapts and integrates three ancient cellular machineries to construct an epithelial cell. The polarized trafficking machinery adapts the cytoskeleton and ancestral secretory and endocytic machineries to the task of sorting and delivering different plasma membrane (PM) proteins to apical and basolateral surface domains. The domain-identity machinery builds a tight junctional fence (TJ) between apical and basolateral PM domains and adapts ancient polarity proteins and polarity lipids on the cytoplasmic side of the PM, which have evolved to perform a diversity of polarity tasks across cells and species, to provide 'identity' to each epithelial PM domain. The 3D organization machinery utilizes adhesion molecules as positional sensors of other epithelial cells and the basement membrane and small GTPases as integrators of positional information with the activities of the domain-identity and polarized trafficking machineries. Cancer is a disease mainly of epithelial cells (90% of human cancers are carcinomas that derive from epithelial cells) that hijacks the EPP machineries, resulting in loss of epithelial polarity, which often correlates in extent with the aggressiveness of the tumor. Here, we review how the EPP integrates its three machineries and the strategies used by cancer to hijack them.

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Section: Polarized Trafficking Machinerymentioning

confidence: 99%

Section: Polarized Trafficking Machinerymentioning

confidence: 99%

The epithelial polarity program: machineries involved and their hijacking by cancer

2008

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“…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]. (B) Kinesin-1 consists of two identical heavy chains and two identical light chains.…”

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

166

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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“…Alternative docking of dynein to organelles is mediated by another dynein LC, Tctex-1, which directly interacts with the C-terminal cytoplasmic end of rhodopsin, which is a candidate gene for retinitis pigmentosa (59). Target proteins of Tctex-1, a 14 kDa LC of dynein, contain a consensus sequence 'R/K-R/K-X-X-R/K' indicating that Tctex-1 binds to its targets in a manner similar to that of DLC8 (60).…”

Section: Myosin Va Is Associated With Melanosomes By Direct Interactimentioning

confidence: 99%

The Dilute Locus and Griscelli Syndrome: Gateways Towards a Better Understanding of Melanosome Transport

Westbroek

Lambert

Naeyaert

2001

Pigment Cell Research

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would present a major breakthrough in the possibilities to In this review an overview of recent advances in the understanding of melanosome movement within epidermal influence pigmentation and related disorders, of great concern melanocytes is given. Exploration of the molecular events to some patients. Moreover, melanosome transport offers a good model to study mammalian organelle trafficking and its involved in and determining the process of melanosome transkey players in general. port, as an essential part of human pigmentation, could lead to the identification of agents that augment, or down-regulate the Key words: Actin, Melanocyte, Motor proteins, Tubulin transfer of melanosomes to surrounding keratinocytes. This in melanosome transport has stagnated somewhat, and the focus was aimed at new molecular families involved in vesicle trafficking. Starting from an overview of the knowledge obtained with relation to molecular motors, the newly discovered involvement and co-operation of other molecules will be summarized in this review. Finally, this collection of findings is depicted graphically in Fig. 1.

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Rhodopsin’s Carboxy-Terminal Cytoplasmic Tail Acts as a Membrane Receptor for Cytoplasmic Dynein by Binding to the Dynein Light Chain Tctex-1

Cited by 455 publications

References 58 publications

The epithelial polarity program: machineries involved and their hijacking by cancer

The epithelial polarity program: machineries involved and their hijacking by cancer

Transport and egress of herpes simplex virus in neurons

The Dilute Locus and Griscelli Syndrome: Gateways Towards a Better Understanding of Melanosome Transport

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