Actin dynamics at the Golgi complex in mammalian cells

Egea, Gustavo; Lázaro‐Diéguez, Francisco; Vilella, Montserrat

doi:10.1016/j.ceb.2006.02.007

Cited by 156 publications

(164 citation statements)

References 117 publications

Supporting

Mentioning

156

Contrasting

Order By: Relevance

“…Furthermore, some htt-interacting proteins, such as HIP-14 (Singaraja et al, 2002) and HIP1R (Carreno et al, 2004), are located in Golgi apparatus. Therefore, it is reasonable to postulate that mhtt could induce aberrant interactions with proteins involved in post-Golgi sorting and trafficking (Egea et al, 2006). Our results also suggest that an incorrect folding attributable to the mutation of the prodomain of BDNF produces an accumulation of Met-BDNF in the Golgi apparatus.…”

Section: Discussionsupporting

confidence: 59%

Mutant huntingtin Impairs the Post-Golgi Trafficking of Brain-Derived Neurotrophic Factor But Not Its Val66Met Polymorphism

Toro¹,

Canals²,

Ginés³

et al. 2006

J. Neurosci.

View full text Add to dashboard Cite

show abstract

Section: Discussionsupporting

confidence: 59%

Mutant huntingtin Impairs the Post-Golgi Trafficking of Brain-Derived Neurotrophic Factor But Not Its Val66Met Polymorphism

Toro¹,

Canals²,

Ginés³

et al. 2006

J. Neurosci.

View full text Add to dashboard Cite

show abstract

“…PKD was also reported to interact with F-actin and cortactin (Eiseler et al, 2007) and to participate in nocodazole-mediated disruption of the Golgi complex (Fuchs et al, 2009). As the morphology of the Golgi complex depends to a large extent on the integrity of the surrounding cytoskeletal elements (Bard and Malhotra, 2006;Egea et al, 2006;De Matteis and Luini, 2008), the observed disruption of the Golgi complex could be also a consequence of altered cytoskeletal organization upon kdPKD1 expression. Additionally, cytoskeletal rearrangements fundamentally influence the formation and maintenance of dendritic structures, including elongation and branching of dendrites or spine formation (Gauthier-Campbell et al, 2004;Kim et al, 2006;Hayashi et al, 2007;Tada et al, 2007;Zhang and Macara, 2008).…”

Section: Discussionmentioning

confidence: 99%

Protein Kinase D Controls the Integrity of Golgi Apparatus and the Maintenance of Dendritic Arborization in Hippocampal Neurons

Czöndör

Ellwanger²,

Fuchs³

et al. 2009

MBoC

View full text Add to dashboard Cite

Protein kinase D (PKD) is known to participate in various cellular functions, including secretory vesicle fission from theGolgi and plasma membrane-directed transport. Here, we report on expression and function of PKD in hippocampal neurons. Expression of an enhanced green fluorescent protein (EGFP)-tagged PKD activity reporter in mouse embryonal hippocampal neurons revealed high endogenous PKD activity at the Golgi complex and in the dendrites, whereas PKD activity was excluded from the axon in parallel with axonal maturation. Expression of fluorescently tagged wild-type PKD1 and constitutively active PKD1 S738/742E (caPKD1) in neurons revealed that both proteins were slightly enriched at the trans-Golgi network (TGN) and did not interfere with its thread-like morphology. By contrast, expression of dominant-negative kinase inactive PKD1 K612W (kdPKD1) led to the disruption of the neuronal Golgi complex, with kdPKD1 strongly localized to the TGN fragments. Similar findings were obtained from transgenic mice with inducible, neuron-specific expression of kdPKD1-EGFP. As a prominent consequence of kdPKD1 expression, the dendritic tree of transfected neurons was reduced, whereas caPKD1 increased dendritic arborization. Our results thus provide direct evidence that PKD activity is selectively involved in the maintenance of dendritic arborization and Golgi structure of hippocampal neurons. INTRODUCTIONNeurons are nondividing and extremely polarized cells, with enormous membrane surface compared with the size of the soma. These features assume a highly specialized secretory machinery, which resembles in certain parts the directed transport mechanisms described in polarized nonneuronal cells (Winckler and Mellman, 1999;Horton and Ehlers, 2004). The vast neuronal membrane surface is functionally and structurally divided into axonal and somatodendritic compartments, possessing specific lipid and protein components required for the spatially different functions, e.g., for pre-or postsynaptic activity (Dresbach et al., 2001;Sheng, 2001;Bresler et al., 2004). The constitutive and precisely directed supply of surface membrane components is indispensable for the function of neurons, especially when considering that postmitotic neurons normally serve throughout the life span of the organism. Up to now, we are far from understanding how the extreme polarization has been evolved and is maintained in neurons.Despite a likely central role in neuronal morphogenesis and membrane trafficking, little is known about the special structure and transport features of the neuronal Golgi apparatus. A thread-like and reticular structure of the Golgi apparatus has been already described in many neuronal types (Takamine et al., 2000;Fujita and Okamoto, 2005;Horton et al., 2005). Central neuronal Golgi complex is localized in the soma and often extends into the principal dendrites, but Golgi elements were also found as discontinuous structures in the distal dendrites, often near synaptic contacts or in dendritic spines (Gardiol et al., 1999;Pierc...

show abstract

“…39 The fact that Cytochalasin B treatment does not dramatically disperse pp65 and RhoB from the AC (Fig. 9A, b, c and e) does not downgrade the importance of actin at this stage of the infection, taking into account the contribution of actin in the structure and function of cellular organelles such as the Golgi and the TGN [79][80][81] that are manipulated by the virus during assembly and perhaps egress. Moreover, actin pattern is remarkably different in cells in which RhoB has been knocked down compared to control cells (Fig.…”

Section: Discussionmentioning

confidence: 99%

RhoB is a component of the human cytomegalovirus assembly complex and is required for efficient viral production

et al. 2015

View full text Add to dashboard Cite

Human Cytomegalovirus (HCMV), an ubiquitous b-herpesvirus, is a significant pathogen that causes medically severe diseases in immunocompromised individuals and in congenitally infected neonates. RhoB belongs to the family of Rho GTPases, which regulates diverse cellular processes. Rho proteins are implicated in the entry and egress from the host cell of mainly a-and g-herpesviruses, whereas b-herpesviruses are the least studied in this regard. Here, we studied the role of RhoB GTPase during HCMV lytic infection. Microscopy analysis, both in fixed and live infected cells showed that RhoB was translocated to the assembly complex/compartment (AC) of HCMV, a cytoplasmic zone in infected cells where many viral structural proteins are known to accumulate and assembly of new virions takes place. Furthermore, RhoB was localized at the AC even when the expression of the late HCMV AC proteins was inhibited. At the very late stages of infection, cellular projections were formed containing RhoB and HCMV virions, potentially contributing to the successful viral spread. Interestingly, the knockdown of RhoB in HCMV-infected cells resulted in a significant reduction of the virus titer and could also affect the accumulation of AC viral proteins at this subcellular compartment. RhoB knockdown also affected actin fibers' structure. Actin reorganization was observed at late stages of infection originating from the viral AC and surrounding the cellular projections, implying a potential interplay between RhoB and actin during HCMV assembly and egress. In conclusion, our results demonstrate for the first time that RhoB is a constituent of the viral AC and is required for HCMV productive infection.

show abstract

Actin dynamics at the Golgi complex in mammalian cells

Cited by 156 publications

References 117 publications

Mutant huntingtin Impairs the Post-Golgi Trafficking of Brain-Derived Neurotrophic Factor But Not Its Val66Met Polymorphism

Mutant huntingtin Impairs the Post-Golgi Trafficking of Brain-Derived Neurotrophic Factor But Not Its Val66Met Polymorphism

Protein Kinase D Controls the Integrity of Golgi Apparatus and the Maintenance of Dendritic Arborization in Hippocampal Neurons

RhoB is a component of the human cytomegalovirus assembly complex and is required for efficient viral production

Contact Info

Product

Resources

About