Porin Is Present in the Plasma Membrane Where It Is Concentrated in Caveolae and Caveolae-related Domains

Báthori, György; Parolini, Isabella; Tombola, Francesco; Szabó, Ildikò; Messina, Angela; Oliva, Marta; Pinto, Vito De; Lisanti, Michael P.; Sargiacomo, Massimo; Zoratti, Mario

doi:10.1074/jbc.274.42.29607

Cited by 114 publications

(98 citation statements)

References 41 publications

(51 reference statements)

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“…It has been documented for several "intracellular" NHE that they can also reside and function on the plasma membrane under certain circumstances, [31][32][33] and dual mitochondrial and plasmalemmal localization has also been reported for the voltage-dependent anion channel VDAC. 34 For the intracellular NHE isoform NHE6, the scaffolding protein RACK1 was recently shown to regulate the balance between plasmalemmal and intracellular localization. 31 Clearly, further studies are needed to elucidate the regulatory pathways underlying this dual localization.…”

Section: Discussionmentioning

confidence: 99%

Characterization of the Sodium/Hydrogen Exchanger NHA2

Fuster¹,

Zhang²,

Shi³

et al. 2008

Journal of the American Society of Nephrology

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Cation/proton exchange has been recognized for decades in mammalian mitochondria, but the exchanger proteins have eluded identification. In this study, a cDNA from a human brain library, previously designated NHA2 in the genome, was cloned and characterized. The NHA2 transcript bears more similarity to prokaryotic than known eukaryotic sodium/proton exchangers, but it was found to be expressed in multiple mammalian organs and cultured cells. A mAb to NHA2 was generated and found to label an approximately 55-kD native protein in multiple tissues and cell lines. The specificity of this antibody was confirmed by demonstrating the loss of the native NHA2 band on immunoblots when cultured cells were treated with NHA2-specific small interfering RNA. Although NHA2 protein was detected in multiple organs, within each, its expression was restricted to specific cell types. In the kidney, co-localization with calbindin 28k and reverse transcription-PCR of microdissected tubules revealed that NHA2 is limited to the distal convoluted tubule. In cell lines, native NHA2 was localized both to the plasma membrane and to the intracellular compartment; immunogold electron microscopy of rat distal convoluted tubule demonstrated NHA2 predominantly but not exclusively on the inner mitochondrial membrane. Furthermore, co-sedimentation of NHA2 antigen and mitochondrial membranes was observed with differential centrifugation, and two mitochondrial markers co-localized with NHA2 in cultured cells. Regarding function, human NHA2 reversed the sodium/hydrogen exchanger-null phenotype when expressed in sodium/hydrogen exchanger-deficient yeast and restored the ability to defend high salinity in the presence of acidic extracellular pH. In summary, NHA2 is a ubiquitous mammalian sodium proton/exchanger that is restricted to the distal convoluted tubule in the kidney.

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Section: Discussionmentioning

confidence: 99%

Characterization of the Sodium/Hydrogen Exchanger NHA2

Fuster¹,

Zhang²,

Shi³

et al. 2008

Journal of the American Society of Nephrology

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“…Some mitochondrial proteins, including the VDAC, prohibitin, and ATP synthase, have been described in association with either the plasma membrane or the surface receptors [38][39][40]. For example, the ATP synthase complex has been located on the surface of a variety of mammalian cells and shown to function as a receptor for angiostatin [41], ApoAI [38], endothelial monocyte-activating polypeptide II [42], and the Vg9Vd2 T-cell receptor [43].…”

Section: Discussionmentioning

confidence: 99%

Oxidation–reduction respiratory chains and ATP synthase complex are localized in detergent-resistant lipid rafts

Ki-Bum

Lee

et al. 2006

Proteomics

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In order to detect and identify ubiquitous lipid raft marker proteins, we isolated lipid rafts from different mouse organs, including the liver, lung, large brain, and kidney, and analyzed their proteins via 2-DE. Many protein spots were determined to be ubiquitous in all of the lipid rafts, and were annotated via LC and MS/MS. Twelve proteins were identified as ubiquitous raft proteins, and most of these were determined to be mitochondrial proteins, including mortalin, prohibitin, voltage-dependent anion channel, ATP synthase, NADH dehydrogenase, and ubiquinol-cytochrome c reductase. Via immunoblotting, these proteins were shown to exist in detergent-resistant lipid rafts prepared using different organ tissues. Since these oxidationreduction respiratory chains and ATP synthase complex were detected in detergent-resistant lipid raft fractions which had been isolated from the plasma membrane but not from the mitochondria, and found in the cell surface when determined by immunofluoresence and immunohistochemistry, we conclude that plasma membrane lipid rafts might contain oxidation-reduction respiratory chains and ATP synthase complex.

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“…Moreover, although several proteins have been identified as mitochondrial or vacuolar, there is evidence that some of these (e.g. ATP synthases [Bae et al, 2004], voltage-dependent anion channels [Bathori et al, 1999], or V-type ATPases [Robinson et al, 1996;Rouquie et al, 1998]) may also have a PM localization. Surprisingly we found a high diversity of ribosomal proteins in the M. truncatula DIM fraction (Table V), similar to a previous study on the Arabidopsis PM (Alexandersson et al, 2004).…”

Section: Proteomic Approach Of the Protein Content Of M Truncatula Rmentioning

confidence: 99%

Characterization of Lipid Rafts from Medicago truncatula Root Plasma Membranes: A Proteomic Study Reveals the Presence of a Raft-Associated Redox System

Furt²,

et al. 2007

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Several studies have provided new insights into the role of sphingolipid/sterol-rich domains so-called lipid rafts of the plasma membrane (PM) from mammalian cells, and more recently from leaves, cell cultures, and seedlings of higher plants. Here we show that lipid raft domains, defined as Triton X-100-insoluble membranes, can also be prepared from Medicago truncatula root PMs. These domains have been extensively characterized by ultrastructural studies as well as by analysis of their content in lipids and proteins. M. truncatula lipid domains are shown to be enriched in sphingolipids and D 7 -sterols, with spinasterol as the major compound, but also in steryl glycosides and acyl-steryl glycosides. A large number of proteins (i.e. 270) have been identified. Among them, receptor kinases and proteins related to signaling, cellular trafficking, and cell wall functioning were well represented whereas those involved in transport and metabolism were poorly represented. Evidence is also given for the presence of a complete PM redox system in the lipid rafts.

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Porin Is Present in the Plasma Membrane Where It Is Concentrated in Caveolae and Caveolae-related Domains

Cited by 114 publications

References 41 publications

Characterization of the Sodium/Hydrogen Exchanger NHA2

Characterization of the Sodium/Hydrogen Exchanger NHA2

Oxidation–reduction respiratory chains and ATP synthase complex are localized in detergent-resistant lipid rafts

Characterization of Lipid Rafts from Medicago truncatula Root Plasma Membranes: A Proteomic Study Reveals the Presence of a Raft-Associated Redox System

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