A signal comprising a basic cluster and an amphipathic α-helix interacts with lipids and is required for the transport of Ist2 to the yeast cortical ER

Maass, Kiran; Fischer, Marcel; Seiler, Markus; Temmerman, Koen; Nickel, Walter; Seedorf, Matthias

doi:10.1242/jcs.036012

Cited by 48 publications

(73 citation statements)

References 46 publications

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“…Point mutations in the intracellular domains of ANO1 can point to the existence of trafficking motifs. The N terminus of ANO1 has been described to be critical for the expression and trafficking of ANO1 to the plasma membrane (41)(42)(43)(44). We identified four mutations in the N terminus that prevented ANO1 from being trafficked to the plasma membrane, opening up the possibility that these residues contribute to a noncanonical trafficking motif in ANO1 and that additional regulatory proteins bind the N terminus and are involved in regulating trafficking of the channel.…”

Section: N Terminus Of Ano1 Regulates Trafficking To the Plasmamentioning

confidence: 97%

Variomics Screen Identifies the Re-entrant Loop of the Calcium-activated Chloride Channel ANO1 That Facilitates Channel Activation

Bill¹,

Popa

Diepen

et al. 2015

Journal of Biological Chemistry

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Background:The calcium-activated chloride channel ANO1 regulates multiple physiological processes. Results: We identified residues that when mutated affected channel activity, intracellular trafficking, or localization and report the first structure-function map of ANO1. Conclusion:The re-entrant loop mediates calcium/voltage sensitivity and activation of ANO1. Significance: We provide new tools for studying ANO1 function in biological systems and its potential as a therapeutic target.

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Section: N Terminus Of Ano1 Regulates Trafficking To the Plasmamentioning

confidence: 97%

Variomics Screen Identifies the Re-entrant Loop of the Calcium-activated Chloride Channel ANO1 That Facilitates Channel Activation

Bill¹,

Popa

Diepen

et al. 2015

Journal of Biological Chemistry

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“…Ist2 is an ER membrane protein in Saccharomyces cerevisiae that acts as an ER-plasma membrane tether (9,10). Yeast lack STIM-ORAI proteins and ER store-dependent calcium signaling, and the Ist2 homologs in mammals-the TMEM16 family-are plasma membrane Cl − channels or phospholipid scramblases (26) that have lost the long unstructured cytoplasmic region and polybasic C-terminal tail essential to the tethering function in the yeast protein (27,28). Thus, there is no reason to expect that Ist2 would interact with STIM, ORAI, or mammalian proteins dedicated to STIM-ORAI signaling.…”

Section: Restoring Junctions Partially Reverses the Effects Of Tmem110mentioning

confidence: 99%

TMEM110 regulates the maintenance and remodeling of mammalian ER–plasma membrane junctions competent for STIM–ORAI signaling

Quintana

Vangipurapu

Farber-Katz

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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The stromal interaction molecule (STIM)–ORAI calcium release-activated calcium modulator (ORAI) pathway controls store-dependent calcium entry, a major mechanism of physiological calcium signaling in mammalian cells. The core elements of the pathway are the regulatory protein STIM1, located in the endoplasmic reticulum (ER) membrane, the calcium channel ORAI1 in the plasma membrane, and sites of close contact between the ER and the plasma membrane that permit the two proteins to interact. Research on calcium signaling has centered on STIM1, ORAI1, and a few proteins that directly modulate STIM–ORAI function. However, little is known about proteins that organize ER–plasma membrane junctions for STIM–ORAI-dependent calcium signaling. Here, we report that an ER-resident membrane protein identified in a previous genome-wide RNAi screen, transmembrane protein 110 (TMEM110), regulates the long-term maintenance of ER–plasma membrane junctions and the short-term physiological remodeling of the junctions during store-dependent calcium signaling.

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“…It was initially believed to be located at the plasma membrane (8)(9)(10)(11), and its cytosolic tail (Ist2ct) has been shown to carry the peripheral targeting signal (8). Ist2ct includes a dimerization domain (amino acids 878-928) and a lysine-rich carboxy terminal tail containing a KKXX-like motif that has been proposed to interact with the PM (11,12).…”

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confidence: 99%

“…The nature of the peripheral Ist2 resident sites remains a matter of debate, however. It was once thought that Ist2 reached the PM in a new Golgi-independent manner (10), but more recently it has been concluded that the major residence site is in fact the cER (11).…”

mentioning

confidence: 99%

Induction of cortical endoplasmic reticulum by dimerization of a coatomer-binding peptide anchored to endoplasmic reticulum membranes

Lavieu

Orci²,

Shi

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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Cortical endoplasmic reticulum (cER) is a permanent feature of yeast cells but occurs transiently in most animal cell types. Ist2p is a transmembrane protein that permanently localizes to the cER in yeast. When Ist2 is expressed in mammalian cells, it induces abundant cER containing Ist2. Ist2 cytoplasmic C-terminal peptide is necessary and sufficient to induce cER. This peptide sequence resembles classic coat protein complex I (COPI) coatomer protein-binding KKXX signals, and indeed the dimerized peptide binds COPI in vitro. Controlled dimerization of this peptide induces cER in cells. RNA interference experiments confirm that coatomer is required for cER induction in vivo, as are microtubules and the microtubule plus-end binding protein EB1. We suggest that Ist2 dimerization triggers coatomer binding and clustering of this protein into domains that traffic at the microtubule growing plus-end to generate the cER beneath the plasma membrane. Sequences similar to the Ist2 lysine-rich tail are found in mammalian STIM proteins that reversibly induce the formation of cER under calcium control

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A signal comprising a basic cluster and an amphipathic α-helix interacts with lipids and is required for the transport of Ist2 to the yeast cortical ER

Abstract: A signal comprising a basic cluster and an amphipathic α-helix interacts with lipids and is required for the transport of Ist2 to the yeast cortical ER

Cited by 48 publications

References 46 publications

Variomics Screen Identifies the Re-entrant Loop of the Calcium-activated Chloride Channel ANO1 That Facilitates Channel Activation

Variomics Screen Identifies the Re-entrant Loop of the Calcium-activated Chloride Channel ANO1 That Facilitates Channel Activation

TMEM110 regulates the maintenance and remodeling of mammalian ER–plasma membrane junctions competent for STIM–ORAI signaling

Induction of cortical endoplasmic reticulum by dimerization of a coatomer-binding peptide anchored to endoplasmic reticulum membranes

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