Receptor and protein kinase C-mediated regulation of ARF binding to the Golgi complex

Matteis, Maria Antonietta De; Santini, Giovanna; Kahn, Richard; Tullio, Giuseppe Di; Luini, Alberto

doi:10.1038/364818a0

Cited by 148 publications

(102 citation statements)

References 36 publications

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“…eRACK/b'COP binds the small ras-like GTPase, ARF, in its GTP-bound form (De Matteis et al, 1993). The GTP-GDP cycle of ARF is linked to COPI recruitment, vesicle binding, and uncoating (De Matteis et al, 1993). We have shown that increased binding of eRACK to Golgi membranes in the presence of GTPgS is associated with an increase in ePKC binding (Csukai et al, 1997).…”

Section: Viral Proteinsmentioning

confidence: 77%

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Adaptor proteins in protein kinase C-mediated signal transduction

2001

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Spatial and temporal organization of signal transduction is essential in determining the speed and precision by which signaling events occur. Adaptor proteins are key to organizing signaling enzymes near their select substrates and away from others in order to optimize precision and speed of response. Here, we describe the role of adaptor proteins in determining the speci®c function of individual protein kinase C (PKC) isozymes. These isozymeselective proteins were called collectively RACKs (receptors for activated C-kinase). The role of RACKs in PKC-mediated signaling was determined using isozyme-speci®c inhibitors and activators of the binding of each isozyme to its respective RACK. In addition to anchoring activated PKC isozymes, RACKs anchor other signaling enzymes. RACK1, the anchoring protein for activated bIIPKC, binds for example, Src tyrosine kinase, integrin, and phosphodiesterase. RACK2, the ePKC-speci®c RACK, is a coated-vesicle protein and thus is involved in vesicular release and cell ± cell communication. Therefore, RACKs are not only adaptors for PKC, but also serve as adaptor proteins for several other signaling enzymes. Because at least some of the proteins that bind to RACKs, including PKC itself, regulate cell growth, modulating their interactions with RACKs may help elucidate signaling pathways leading to carcinogenesis and could result in the identi®cation of novel therapeutic targets. Oncogene (2001) 20, 6339 ± 6347.

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Section: Viral Proteinsmentioning

confidence: 77%

“…However, eRACK is part of the coatomer complex, COPI, and therefore binds to a number of other proteins. eRACK/b'COP binds the small ras-like GTPase, ARF, in its GTP-bound form (De Matteis et al, 1993). The GTP-GDP cycle of ARF is linked to COPI recruitment, vesicle binding, and uncoating (De Matteis et al, 1993).…”

Section: Viral Proteinsmentioning

confidence: 99%

Adaptor proteins in protein kinase C-mediated signal transduction

2001

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“…Therefore, it is feasible that Rap1A directly binds to, and thereby stimulates PLCe in the Golgi apparatus in response to extracellular stimuli such as EGF treatment. Considering that protein kinase C exists in the Golgi apparatus (de Matteis et al, 1993), and can act as a downstream target of DAG yielded by PLCe, the Rap1A/PLCe signaling pathway may provide a link between growth factor receptors and Golgi-localized protein kinase C.…”

Section: Discussionmentioning

confidence: 99%

Differential roles of Ras and Rap1 in growth factor-dependent activation of phospholipase Cε

et al. 2002

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“…PMA-induced translocation of ARF to the Golgi membrane has already been described [50]. PMA also induced a massive translocation of PKC␣.…”

Section: Discussionmentioning

confidence: 84%

Tyrosine kinase-regulated small GTPase translocation and the activation of phospholipase D in HL60 granulocytes

Houle

Naccache

Bourgoin

1999

Journal of Leukocyte Biology

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We focus on the mechanisms of regulation of phospholipase D (PLD) activity. Three agonists known to stimulate PLD activity, fMet-LeuPhe (fMLP), phorbol 12-myristate 13-acetate (PMA) and V 4؉ -OOH, induced a differential translocation of ADP-ribosylation factor (ARF), RhoA, and protein kinase C␣ (PKC␣), all cofactors for PLD activation. Whereas fMLP recruited all three proteins to membranes, V 4؉ -OOH only elicited RhoA translocation and PMA induced ARF and PKC␣ translocation. Three tyrosine kinases inhibitors, ST-638, methyl 2,5-dihydroxycinnamate, and genistein reduced fMLP-stimulated PLD activity by up to 80%. Furthermore, tyrosine kinase inhibitors reduced the fMLP-induced increase of GTP␥S-stimulated PLD activity in membranes and recruitment of ARF, RhoA, and PKC␣ to the membrane fraction. The data suggest that a tyrosine phosphorylation event is located upstream of the translocation of ARF, RhoA, and PKC␣ in the signaling pathway leading to PLD activation by fMLP. RO 31-8220, a specific inhibitor of PKC, reduced PMA-induced PLD activity by 80% in intact HL60 granulocytes but enhanced fMLP-stimulated PLD activity by 60%. Although PMA alone had no effect on RhoA recruitment to the membrane fraction, in the presence of RO 31-8220 the levels of membrane-bound RhoA were increased. The levels of membrane-bound ARF and PKC␣ were unaffected by RO 31-8220 during PMA stimulation. In contrast, fMLP-induced recruitment of ARF and RhoA was insensitive to RO 31-8220 but PKC␣ translocation was increased. We propose that RhoA translocation may be regulated by PKC in an ATPindependent manner. Furthermore, increased fMLP-induced PKC␣ translocation in the presence of RO 31-8220 may partially account for the synergistic activation of PLD observed when both fMLP and RO 31-8220 are used together in intact HL60 cells.

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Receptor and protein kinase C-mediated regulation of ARF binding to the Golgi complex

Cited by 148 publications

References 36 publications

Adaptor proteins in protein kinase C-mediated signal transduction

Adaptor proteins in protein kinase C-mediated signal transduction

Differential roles of Ras and Rap1 in growth factor-dependent activation of phospholipase Cε

Tyrosine kinase-regulated small GTPase translocation and the activation of phospholipase D in HL60 granulocytes

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