Actin microfilaments are essential for the cytological positioning and morphology of the Golgi complex

Valderrama, Ferran; Babià, T; Ayala, Inmaculada; Renau‐Piqueras, Jaime; Egea, Gustavo

doi:10.1016/s0171-9335(98)80012-5

Cited by 125 publications

(115 citation statements)

References 58 publications

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“…It is therefore not surprising that actin-depolymerizing drugs have been shown to disrupt both Golgi morphology and positioning [11,12]. Perhaps more surprising is that most of these proteins rapidly dissociate from the Golgi upon treatment of cells with brefeldin A (BFA), a fungal toxin that selectively inhibits Golgi-associated Arf nucleotide exchange factors.…”

Section: Arf Regulation Of Actin Assembly In the Golgimentioning

confidence: 99%

Regulation of actin cytoskeleton dynamics by Arf-family GTPases

Myers

Casanova

2008

Trends in Cell Biology

165

139

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Small GTPases of the Arf family are best known for their role in vesicular transport, wherein they nucleate the assembly of coat proteins at sites of carrier vesicle formation. However, accumulating evidence indicates that the Arfs are also important regulators of actin cytoskeleton dynamics and are involved in a variety of actin-based processes, including cell adhesion, migration and neurite outgrowth. The mechanisms of this regulation are remarkably diverse, ranging from the integration of vesicular transport with cytoskeleton assembly to the direct regulation of Rho-family GTPase function. Here, we review recent progress in our understanding of how Arfs and their interacting proteins function to integrate membrane and cytoskeletal dynamics.

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Section: Arf Regulation Of Actin Assembly In the Golgimentioning

confidence: 99%

Regulation of actin cytoskeleton dynamics by Arf-family GTPases

Myers

Casanova

2008

Trends in Cell Biology

165

139

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“…These disparate results are due to the fact that, unlike LtB and C2 toxin, CyD does not appear to produce a significant net depolymerization of F-actin [Morris and Tannenbaum, 1980]. However, when examining the effect of actin toxins on Golgi morphology, these three F-actin disrupters (CyD, LtB and C2 toxin) caused the same compaction of the Golgi complex [Valderrama et al, 2001], which occurred before the rounding up of cells [Valderrama et al, 1998[Valderrama et al, , 2001. Thus, results obtained with these three F-actin depolimerizing agents indicate that there is a high sensitivity of the Golgi shape to changes in the organization of the actin cytoskeleton but it is not always necessarily followed by alterations in the Golgi-associated membrane dynamics or protein transport [di Campli et al, 1999].…”

Section: Introductionmentioning

confidence: 95%

“…Indirect immunofluorescence was carried out as described previously [Valderrama et al, 1998[Valderrama et al, , 2000 with the following antibody dilutions: anti-giantin, 1:500 and goat anti-mouse FITC, 1:50. TRITC-phalloidin was used at 1:500.…”

Section: Indirect Immunofluorescencementioning

confidence: 99%

“…We have previously reported that the disruption of actin filaments causes compaction of the Golgi complex in NRK cells [Valderrama et al, 1998[Valderrama et al, , 2001. However, it is not known (i) whether this unusual Golgi morphology is generated in other mammalian cell lines when the actin cytoskeleton is disrupted by actin toxins and (ii) whether different toxins cause equivalent alterations of Golgi ultrastructure.…”

Section: All Anti-actin Agents Induce Compaction Of the Golgi Complexmentioning

confidence: 99%

“…However, it is important to utilize more than one actin toxin because depending on the anti-actin agent used, disparate results are obtained. For instance, on the basis of results obtained using cytochalasin D (CyD) we initially reported that membrane dynamics at the ER/Golgi interface was actin-independent [Valderrama et al, 1998]. In contrast, in a subsequent study, using latrunculin B (LtB) or Clostridium botulinum C2 toxin (C2 toxin), we reported that microfilaments were involved in the retrograde (Golgi-to-ER) but not anterograde (ER-to-Golgi) membrane pathway [Valderrama et al, 2001].…”

Section: Introductionmentioning

confidence: 99%

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Actin filaments are involved in the maintenance of Golgi cisternae morphology and intra‐Golgi pH

Lázaro‐Diéguez

Jiménez

Barth

et al. 2006

Cell Motil. Cytoskeleton

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Here we examine the contribution of actin dynamics to the architecture and pH of the Golgi complex. To this end, we have used toxins that depolymerize (cytochalasin D, latrunculin B, mycalolide B, and Clostridium botulinum C2 toxin) or stabilize (jasplakinolide) filamentous actin. When various clonal cell lines were examined by epifluorescence microscopy, all of these actin toxins induced compaction of the Golgi complex. However, ultrastructural analysis by transmission electron microscopy and electron tomography/three-dimensional modelling of the Golgi complex showed that F-actin depolymerization first induces perforation/fragmentation and severe swelling of Golgi cisternae, which leads to a completely disorganized structure. In contrast, F-actin stabilization results only in cisternae perforation/fragmentation. Concomitantly to actin depolymerization-induced cisternae swelling and disorganization, the intra-Golgi pH significantly increased. Similar ultrastructural and Golgi pH alkalinization were observed in cells treated with the vacuolar H þ -ATPases inhibitors bafilomycin A1 and concanamycin A. Overall, these results suggest that actin filaments are implicated in the preservation of the flattened shape of Golgi cisternae. This maintenance seems to be mediated by the regulation of the state of F-actin assembly on the Golgi pH homeostasis. Cell Motil. Cytoskeleton 63: 778-791, 2006. '

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Vesicle transport: The role of actin filaments and myosin motors

DePina

Langford

1999

Microsc. Res. Tech.

135

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The transport of vesicles and the retention of organelles at specific locations are fundamental processes in cells. Actin filaments and myosin motors have been shown to be required for both of these tasks. Most of the organelles in cells associate with actin filaments and some of the myosin motors required for movement on actin filaments have been identified. Myosin V has been shown to transport endoplasmic reticulum (ER) vesicles in neurons, pigment granules in melanocytes, and the vacuole in yeast. Myosin I has been shown to be involved in the transport of Golgi‐derived vesicles in epithelial cells. Myosin VI has been shown to be associated with Golgi‐derived vesicles, and cytoplasmic vesicles in living Drosophila embryos. Myosin II may be a vesicle motor but its role in vesicle transport has not been resolved. Secretory vesicles, endosomes and mitochondria appear to be transported on actin filaments but the myosin motors on these organelles have not been identified. Mitochondria in yeast may be transported by the dynamic assembly of an actin “tail.” The model that has unified all of these findings is the concept that long‐range movement of vesicles occurs on microtubules and short‐range movement on actin filaments. The details of how the microtubule‐dependent and the actin‐dependent motors are coordinated are important questions in the field. There is now strong evidence that two molecular motors, kinesin and myosin V, interact with each other and perhaps function as a complex on vesicles. An understanding of the interrelationship of microtubules and actin filaments and the motors that move cargo on them will ultimately establish how vesicles and organelles are transported to their specific locations in cells. Microsc. Res. Tech. 47:93–106, 1999. © 1999 Wiley‐Liss, Inc.

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Actin microfilaments are essential for the cytological positioning and morphology of the Golgi complex

Cited by 125 publications

References 58 publications

Regulation of actin cytoskeleton dynamics by Arf-family GTPases

Regulation of actin cytoskeleton dynamics by Arf-family GTPases

Actin filaments are involved in the maintenance of Golgi cisternae morphology and intra‐Golgi pH

Vesicle transport: The role of actin filaments and myosin motors

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