Cholesterol-dependent Localization of NAP-22 on a Neuronal Membrane Microdomain (Raft)

Maékawa, Shohei; Sato, Chihiro; Kitajima, Ken; Funatsu, Nobuo; Kumanogoh, Haruko; Sokawa, Yoshihiro

doi:10.1074/jbc.274.30.21369

Cited by 96 publications

(86 citation statements)

References 63 publications

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“…It has been suggested that this cell membrane-Golgi pathway may regulate lipid raft distribution and function with recycling occurring continuously (51). Amyloid precursor protein and A␤ are associated with cholesterol-rich low density membrane domains (52)(53)(54)(55). Extracellular A␤ that is not highly aggregated may target lipid rafts, promoting cycling of lipid rafts to the Golgi complex.…”

Section: Discussionmentioning

confidence: 99%

Cholesterol Distribution in the Golgi Complex of DITNC1 Astrocytes Is Differentially Altered by Fresh and Aged Amyloid औ-Peptide-(1–42)

Igbavboa

Pidcock

Johnson

et al. 2003

Journal of Biological Chemistry

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The Golgi complex plays an important role in cholesterol trafficking in cells, and amyloid ␤-peptides (A␤s) alter cholesterol trafficking. The hypothesis was tested that fresh and aged A␤-(1-42) would differentially modify Golgi cholesterol content in DINTC1 astrocytes and that the effects of A␤-(1-42) would be associated with the region of the Golgi complex. Two different methods were used to determine the effects of A␤-(1-42) on Golgi complex cholesterol. Confocal microscopy showed that fresh A␤-(1-42) significantly increased cholesterol and that aged A␤-(1-42) significantly reduced cholesterol content in the Golgi complex. Isolation of the Golgi complex into two fractions using density gradient centrifugation showed effects of aged A␤-(1-42) similar to those observed with confocal microscopy but revealed the novel finding that fresh A␤-(1-42) had opposite effects on the two Golgi fractions suggesting a specificity of A␤-(1-42) perturbation of the Golgi complex. Phosphatidylcholine-phospholipase D activity, cell membrane cholesterol, and apolipoprotein E levels were associated with effects of fresh A␤-(1-42) on cholesterol distribution but not with effects of aged A␤-(1-42), arguing against a common mechanism. Extracellular A␤-(1-42) targets the Golgi complex and disrupts cell cholesterol homeostasis, and this action of A␤-(1-42) could alter cell functions requiring optimal levels of cholesterol.

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Section: Discussionmentioning

confidence: 99%

Cholesterol Distribution in the Golgi Complex of DITNC1 Astrocytes Is Differentially Altered by Fresh and Aged Amyloid औ-Peptide-(1–42)

Igbavboa

Pidcock

Johnson

et al. 2003

Journal of Biological Chemistry

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“…However, this distribution was disrupted by cholesterol depletion with methyl‐β‐cyclodextrin (βMCD), a procedure known to disrupt lipid rafts (Maekawa et al . 1999). Similarly, co‐immunoprecipitation and PLA experiments revealed that the cholesterol depletion disrupted the interaction between ANO1 and IP 3 R1 in DRG neurons.…”

Section: Coupling Between Ano1 and Endoplasmic Reticulum; Is This A Gmentioning

confidence: 99%

Activation of Ca²⁺‐activated Cl⁻ channel ANO1 by localized Ca²⁺ signals

Jin

Shah

et al. 2014

The Journal of Physiology

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Ca2+‐activated chloride channels (CaCCs) regulate numerous physiological processes including epithelial transport, smooth muscle contraction and sensory processing. Anoctamin‐1 (ANO1, TMEM16A) is a principal CaCC subunit in many cell types, yet our understanding of the mechanisms of ANO1 activation and regulation are only beginning to emerge. Ca2+ sensitivity of ANO1 is rather low and at negative membrane potentials the channel requires several micromoles of intracellular Ca2+ for activation. However, global Ca2+ levels in cells rarely reach such levels and, therefore, there must be mechanisms that focus intracellular Ca2+ transients towards the ANO1 channels. Recent findings indeed indicate that ANO1 channels often co‐localize with sources of intracellular Ca2+ signals. Interestingly, it appears that in many cell types ANO1 is particularly tightly coupled to the Ca2+ release sites of the intracellular Ca2+ stores. Such preferential coupling may represent a general mechanism of ANO1 activation in native tissues.

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“…Solubilization of PDE with MCD Extraction-It is known that the cholesterol-removing regent, methyl-␤-cyclodextrin, can solubilize a certain protein component of the Triton X-100-resistant membrane of rat brain (18). Thus, we examined the effect of MCD on the protein composition of DRM derived from light-and GTP␥S-exposed ROS.…”

Section: Rafts In Retinal Photoreceptors 20814mentioning

confidence: 99%

Light- and Guanosine 5′-3-O-(Thio)triphosphate-sensitive Localization of a G Protein and Its Effector on Detergent-resistant Membrane Rafts in Rod Photoreceptor Outer Segments

Seno

Kishimoto

Abe

et al. 2001

Journal of Biological Chemistry

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Detergent-resistant membrane microdomains in the plasma membrane, known as lipid rafts, have been implicated in various cellular processes. We report here that a low-density Triton X-100-insoluble membrane (detergent-resistant membrane; DRM) fraction is present in bovine rod photoreceptor outer segments (ROS). In dark-adapted ROS, transducin and most of cGMPphosphodiesterase (PDE) were detergent-soluble. When ROS membranes were exposed to light, however, a large portion of transducin localized in the DRM fraction. Furthermore, on addition of guanosine 5-3-O-(thio)triphosphate (GTP␥S) to light-bleached ROS, transducin became detergent-soluble again. PDE was not recruited to the DRM fraction after light stimulus alone, but simultaneous stimulation by light and GTP␥S induced a massive translocation of all PDE subunits to the DRM. A cholesterol-removing reagent, methyl-␤-cyclodextrin, selectively but partially solubilized PDE from the DRM, suggesting that cholesterol contributes, at least in part, to the association of PDE with the DRM. By contrast, transducin was not extracted by the depletion of cholesterol. These data suggest that transducin and PDE are likely to perform their functions in phototransduction by changing their localization between two distinct lipid phases, rafts and surrounding fluid membrane, on disc membranes in an activation-dependent manner.The phototransduction system in the photoreceptor rod outer segments (ROS) 1 of vertebrates is a typical G protein-mediated signaling system. In the prevailing model of phototransduction (1), light-excited rhodopsin interacts with the GDP form of the heterotrimeric G protein transducin and stimulates GDP-GTP exchange on its ␣-subunit (T ␣ ). GTP-T ␣ separates from its counterpart, the ␤␥ subunit of transducin (T ␤␥ ), and binds the inhibitory subunit (P ␥ ) of cGMP-phosphodiesterase (PDE), thus releasing the constraint of P ␥ on the catalytic subunits (P ␣ and P ␤ ) of PDE. The resulting decrease in cytoplasmic cGMP leads to the closure of cGMP-gated channels and the hyperpolarization of photoreceptor plasma membranes. Although the signaling cascade of ROS has been intensively studied during the past two decades, the whole mechanism has not yet been elucidated (for review see Ref.2).

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Cholesterol-dependent Localization of NAP-22 on a Neuronal Membrane Microdomain (Raft)

Cited by 96 publications

References 63 publications

Cholesterol Distribution in the Golgi Complex of DITNC1 Astrocytes Is Differentially Altered by Fresh and Aged Amyloid औ-Peptide-(1–42)

Cholesterol Distribution in the Golgi Complex of DITNC1 Astrocytes Is Differentially Altered by Fresh and Aged Amyloid औ-Peptide-(1–42)

Activation of Ca²⁺‐activated Cl⁻ channel ANO1 by localized Ca²⁺ signals

Light- and Guanosine 5′-3-O-(Thio)triphosphate-sensitive Localization of a G Protein and Its Effector on Detergent-resistant Membrane Rafts in Rod Photoreceptor Outer Segments

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Cholesterol-dependent Localization of NAP-22 on a Neuronal Membrane Microdomain (Raft)

Cited by 96 publications

References 63 publications

Cholesterol Distribution in the Golgi Complex of DITNC1 Astrocytes Is Differentially Altered by Fresh and Aged Amyloid औ-Peptide-(1–42)

Cholesterol Distribution in the Golgi Complex of DITNC1 Astrocytes Is Differentially Altered by Fresh and Aged Amyloid औ-Peptide-(1–42)

Activation of Ca2+‐activated Cl− channel ANO1 by localized Ca2+ signals

Light- and Guanosine 5′-3-O-(Thio)triphosphate-sensitive Localization of a G Protein and Its Effector on Detergent-resistant Membrane Rafts in Rod Photoreceptor Outer Segments

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Activation of Ca²⁺‐activated Cl⁻ channel ANO1 by localized Ca²⁺ signals