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Book ; Conference proceedings: Calcium signaling: from stores to channels

Putney, James W. / Bird, Gary S.

honoring James W. Putney Jr : July 31st-August 3rd, 2016, The Carolina Inn, Chapel Hill, NC

(Cell calcium ; volume 63=Special issue (May 2017))

2017

Event/congress	International Conference on Calcium Signaling: From Stores to Channels (2016, ChapelHillNC)
Author's details	guest editors: Dr. Gary S. Bird, Dr. Shmuel Muallem ; International Conference on Calcium Signaling: From Stores to Channels
Series title	Cell calcium ; volume 63=Special issue (May 2017)
Collection
Language	English
Size	96 Seiten, Illustrationen, Diagramme
Publisher	Elsevier
Publishing place	Amsterdam
Publishing country	Netherlands
Document type	Book ; Conference proceedings
HBZ-ID	HT019395880
Database	Catalogue ZB MED Medicine, Health

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Zs A 1596 -63-	not available for loan	Zeitschriften-Lesesaal

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Article: Calcium Signaling: Septins Organize the SOC Channel

Putney, James W., Jr

Current biology. 2013 Aug. 19, v. 23, no. 16

2013

Abstract: Store-operated Ca²⁺ entry is a widely encountered mechanism for generating cytoplasmic Ca²⁺ signals. From a whole-genome screen in HeLa cells, a new study reveals that cytoskeletal septins play a critical role in this process, by organizing signaling ... ...

Abstract	Store-operated Ca²⁺ entry is a widely encountered mechanism for generating cytoplasmic Ca²⁺ signals. From a whole-genome screen in HeLa cells, a new study reveals that cytoskeletal septins play a critical role in this process, by organizing signaling structures in the plasma membrane.
Keywords	calcium signaling ; cytoskeleton ; plasma membrane
Language	English
Dates of publication	2013-0819
Size	p. R684-R685.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2013.07.042
Database	NAL-Catalogue (AGRICOLA)

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Article: New molecular players in capacitative Ca²⁺ entry

Putney, James W. Jr

Journal of cell science. 2007 June 15, v. 120, no. 12

2007

Abstract: Capacitative Ca²⁺ entry links the emptying of intracellular Ca²⁺ stores to the activation of store-operated Ca²⁺ channels in the plasma membrane. In the twenty years since the inception of the concept of capacitative Ca²⁺ entry, a number of activation ... ...

Abstract	Capacitative Ca²⁺ entry links the emptying of intracellular Ca²⁺ stores to the activation of store-operated Ca²⁺ channels in the plasma membrane. In the twenty years since the inception of the concept of capacitative Ca²⁺ entry, a number of activation mechanisms have been proposed, and there has been considerable interest in the possibility that TRP channels function as store-operated channels. However, in the past two years, two major players in both the signaling and permeation mechanisms for store-operated channels have been discovered: Stim1 and the Orai proteins. Stim1 is an endoplasmic reticulum Ca²⁺ sensor. It appears to act by redistributing within a small component of the endoplasmic reticulum, approaching the plasma membrane, but does not seem to translocate into the plasma membrane. Stim1 signals to plasma membrane Orai proteins, which constitute pore-forming subunits of store-operated channels.
Language	English
Dates of publication	2007-0615
Size	p. 1959-1965.
Publishing place	The Company of Biologists Limited
Document type	Article
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
Database	NAL-Catalogue (AGRICOLA)

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Article: Calcium signaling in osteoclasts

Hwang, Sung-Yong / Putney, James W., Jr

Biochimica et biophysica acta. Molecular cell research. 2011 May, v. 1813, no. 5

2011

Abstract: It has long been known that many bone diseases, including osteoporosis, involve abnormalities in osteoclastic bone resorption. As a result, there has been intense study of the mechanisms that regulate both the differentiation and bone resorbing function ... ...

Abstract	It has long been known that many bone diseases, including osteoporosis, involve abnormalities in osteoclastic bone resorption. As a result, there has been intense study of the mechanisms that regulate both the differentiation and bone resorbing function of osteoclast cells. Calcium (Ca2+) signaling appears to play a critical role in the differentiation and functions of osteoclasts. Cytoplasmic Ca2+ oscillations occur during RANKL-mediated osteoclastogenesis. Ca2+ oscillations provide a digital Ca2+ signal that induces osteoclasts to up-regulate and autoamplify nuclear factor of activated T cells c1 (NFATc1), a Ca2+/calcineurin-dependent master regulator of osteoclastogenesis. Here we review previous studies on Ca2+ signaling in osteoclasts as well as recent breakthroughs in understanding the basis of RANKL-induced Ca2+ oscillations, and we discuss possible molecular players in this specialized Ca2+ response that appears pivotal for normal bone function. This article is part of a Special Issue entitled: 11th European Symposium on Calcium.
Keywords	T-lymphocytes ; bone resorption ; calcium ; calcium signaling ; osteoclasts ; osteoporosis
Language	English
Dates of publication	2011-05
Size	p. 979-983.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	283444-3
ISSN	0167-4889
ISSN	0167-4889
DOI	10.1016/j.bbamcr.2010.11.002
Database	NAL-Catalogue (AGRICOLA)

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Article: Phosphoregulation of STIM1 Leads to Exclusion of the Endoplasmic Reticulum from the Mitotic Spindle

Smyth, Jeremy T / Beg, Amber M / Wu, Shilan / Putney, James W., Jr / Rusan, Nasser M

Current biology. 2012 Aug. 21, v. 22, no. 16

2012

Abstract: The endoplasmic reticulum (ER) undergoes significant reorganization between interphase and mitosis, but the underlying mechanisms are unknown [1]. Stromal interaction molecule 1 (STIM1) is an ER Ca²⁺ sensor that activates store-operated Ca²⁺ entry (SOCE) ...

Abstract	The endoplasmic reticulum (ER) undergoes significant reorganization between interphase and mitosis, but the underlying mechanisms are unknown [1]. Stromal interaction molecule 1 (STIM1) is an ER Ca²⁺ sensor that activates store-operated Ca²⁺ entry (SOCE) [2, 3] and also functions in ER morphogenesis through its interaction with the microtubule +TIP protein end binding 1 (EB1) [4]. We previously demonstrated that phosphorylation of STIM1 during mitosis suppresses SOCE [5]. We now show that STIM1 phosphorylation is a major regulatory mechanism that excludes ER from the mitotic spindle. In mitotic HeLa cells, the ER forms concentric sheets largely excluded from the mitotic spindle. We show that STIM1 dissociates from EB1 in mitosis and localizes to the concentric ER sheets. However, a nonphosphorylatable STIM1 mutant (STIM1¹⁰ᴬ) colocalized extensively with EB1 and drove ER mislocalization by pulling ER tubules into the spindle. This effect was rescued by mutating the EB1 interaction site of STIM1¹⁰ᴬ, demonstrating that aberrant association of STIM1¹⁰ᴬ with EB1 is responsible for the ER mislocalization. A STIM1 phosphomimetic exhibited significantly impaired +TIP tracking in interphase but was ineffective at inhibiting SOCE, suggesting different mechanisms of regulation of these two STIM1 functions by phosphorylation. Thus, ER spindle exclusion and ER-dependent Ca²⁺ signaling during mitosis require multimodal STIM1 regulation by phosphorylation.
Keywords	endoplasmic reticulum ; interphase ; mitosis ; mitotic spindle apparatus ; morphogenesis ; mutants ; phosphorylation
Language	English
Dates of publication	2012-0821
Size	p. 1487-1493.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2012.05.057
Database	NAL-Catalogue (AGRICOLA)

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Article: Deletion of Orai1 alters expression of multiple genes during osteoclast and osteoblast maturation

Hwang, Sung-Yong / Foley, Julie / Numaga-Tomita, Takuro / Petranka, John G / Bird, Gary S / Putney, James W., Jr

Cell calcium. 2012 Dec., v. 52, no. 6

2012

Abstract: Store-operated Ca2+ entry (SOCE) is a major Ca2+ influx pathway in most non-excitable cell types and Orai1 was recently identified as an essential pore-subunit of SOCE channels. Here we investigate the physiological role of Orai1 in bone homeostasis ... ...

Abstract	Store-operated Ca2+ entry (SOCE) is a major Ca2+ influx pathway in most non-excitable cell types and Orai1 was recently identified as an essential pore-subunit of SOCE channels. Here we investigate the physiological role of Orai1 in bone homeostasis using Orai1-deficient mice (Orai1−/−). Orai1−/− mice developed osteopenia with decreased bone mineral density and trabecular bone volume. To identify the nature and origin of the bone defect, bone-resorbing osteoclasts and bone-forming osteoblasts from Orai1−/− mice were examined. Orai1-mediated SOCE was completely abolished in Orai1−/− osteoclast precursor cells and osteoclastogenesis in vitro from Orai1−/− mice was impaired due to a defect in cell fusion of pre-osteoclasts. Also, resorption activity in vitro was comparable but the size of pits formed by Orai1−/− osteoclasts was smaller. We next assessed the role of Orai1 in osteoblast differentiation and function by using a pre-osteoblast cell line, as well as primary osteoblasts from wild-type and Orai1−/− mice. SOCE in MC3T3-E1 pre-osteoblastic cells was inactivated by lentiviral overexpression of a pore-dead Orai1 mutant. Lack of SOCE in MC3T3-E1 had no effect on alkaline phosphatase staining and expression but substantially inhibited mineralized nodule formation. Consistent with this finding, Orai1-mediated SOCE was markedly reduced in Orai1−/− osteoblast precursor cells and osteoblastogenesis in vitro from Orai1−/− stromal cells showed impaired mineral deposition but no change in differentiation. This indicates that Orai1 is involved in the function but not in the differentiation of osteoblasts. Together, these results suggest that Orai1 plays a critical role in bone homeostasis by regulating both osteoblasts and osteoclasts.
Keywords	alkaline phosphatase ; bone density ; calcium ; cell fusion ; gene overexpression ; genes ; homeostasis ; mice ; mineralization ; mutants ; osteoblasts ; osteoclasts ; osteopenia ; resorption ; stromal cells
Language	English
Dates of publication	2012-12
Size	p. 488-500.
Publishing place	Elsevier India Pvt Ltd.
Document type	Article
ZDB-ID	757687-0
ISSN	1532-1991 ; 0143-4160
ISSN (online)	1532-1991
ISSN	0143-4160
DOI	10.1016/j.ceca.2012.10.001
Database	NAL-Catalogue (AGRICOLA)

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Article: Ca²⁺-store-dependent and -independent reversal of Stim1 localization and function

Smyth, Jeremy T / DeHaven, Wayne I / Bird, Gary S / Putney, James W. Jr

Journal of cell science. 2008 Mar. 15, v. 121, no. 6

2008

Abstract: Stim1 responds to depletion of ER Ca²⁺ stores by rearranging from tubular structures throughout the ER into punctate structures near the plasma membrane, where it activates Orai store-operated Ca²⁺ entry (SOCE) channels. However, the mechanism and ... ...

Abstract	Stim1 responds to depletion of ER Ca²⁺ stores by rearranging from tubular structures throughout the ER into punctate structures near the plasma membrane, where it activates Orai store-operated Ca²⁺ entry (SOCE) channels. However, the mechanism and structural determinants of the localization and reversal of Stim1 puncta formation are poorly understood. Using HEK293 cells expressing Stim1 tagged with enhanced yellow fluorescent protein (EYFP-Stim1), we show that the basis for SOCE termination is the reversal of the punctate Stim1 localization, which absolutely depends on SOCE-dependent store refilling. We also describe rapid, store-independent reversal of EYFP-Stim1 punctae by the ML-9 inhibitor of myosin-light-chain kinase (MLCK). ML-9 similarly inhibited SOCE and the Ca²⁺-release-activated Ca²⁺ (CRAC) current. Reversal by ML-9 resulted in full re-establishment of the tubular EYFP-Stim1 localization. A constitutively active EF-hand mutant of EYFP-Stim1 was also reversed by ML-9, regardless of the Ca²⁺ store content. Inhibition by ML-9 was not due to MLCK inhibition as other inhibitors of MLCK had no effect. Finally, we provide evidence that EYFP-Stim1 punctae form in specific predetermined cellular loci. We conclude that SOCE is tightly coupled to formation of Stim1 puncta, and both SOCE and puncta formation involve a dynamic, reversible signaling complex that probably consists of components in addition to Stim1 and Orai channels.
Language	English
Dates of publication	2008-0315
Size	p. 762-772.
Publishing place	The Company of Biologists Limited
Document type	Article
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
Database	NAL-Catalogue (AGRICOLA)

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Article: Role of the microtubule cytoskeleton in the function of the store-operated Ca²⁺ channel activator STIM1

Smyth, Jeremy T / DeHaven, Wayne I / Bird, Gary S / Putney, James W. Jr

Journal of cell science. 2007 Nov. 1, v. 120, no. 21

2007

Abstract: We examined the role of the microtubule cytoskeleton in the localization and store-operated Ca²⁺ entry (SOCE) function of the endoplasmic reticulum (ER) Ca²⁺ sensor stromal interaction molecule 1 (STIM1) in HEK 293 cells. STIM1 tagged with an enhanced ... ...

Abstract	We examined the role of the microtubule cytoskeleton in the localization and store-operated Ca²⁺ entry (SOCE) function of the endoplasmic reticulum (ER) Ca²⁺ sensor stromal interaction molecule 1 (STIM1) in HEK 293 cells. STIM1 tagged with an enhanced yellow fluorescent protein (EYFP-STIM1) exhibited a fibrillar localization that colocalized with endogenous α-tubulin. Depolymerization of microtubules with nocodazole caused a change from a fibrillar EYFP-STIM1 localization to one that was similar to that of the ER. Treatment of HEK 293 cells with nocodazole had a detrimental impact on SOCE and the associated Ca²⁺ release-activated Ca²⁺ current (ICRAC). This inhibition was significantly reversed in cells overexpressing EYFP-STIM1, implying that the primary inhibitory effect of nocodazole is related to STIM1 function. Surprisingly, nocodazole treatment alone induced significant SOCE and ICRAC in cells expressing EYFP-STIM1, and this was accompanied by an increase in EYFP-STIM1 fluorescence near the plasma membrane. We conclude that microtubules play a facilitative role in the SOCE signaling pathway by optimizing the localization of STIM1.
Language	English
Dates of publication	2007-1101
Size	p. 3762-3771.
Publishing place	The Company of Biologists Limited
Document type	Article
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
Database	NAL-Catalogue (AGRICOLA)

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Article: Complex Actions of 2-Aminoethyldiphenyl Borate on Store-operated Calcium Entry

DeHaven, Wayne I / Smyth, Jeremy T / Boyles, Rebecca R / Bird, Gary S / Putney, James W. Jr

Journal of biological chemistry. 2008 July 11, v. 283, no. 28

2008

Abstract: Store-operated Ca²⁺ entry (SOCE) is likely the most common mode of regulated influx of Ca²⁺ into cells. However, only a limited number of pharmacological agents have been shown to modulate this process. 2-Aminoethyldiphenyl borate (2-APB) is a widely ... ...

Abstract	Store-operated Ca²⁺ entry (SOCE) is likely the most common mode of regulated influx of Ca²⁺ into cells. However, only a limited number of pharmacological agents have been shown to modulate this process. 2-Aminoethyldiphenyl borate (2-APB) is a widely used experimental tool that activates and then inhibits SOCE and the underlying calcium release-activated Ca²⁺ current (ICRAC). The mechanism by which depleted stores activates SOCE involves complex cellular movements of an endoplasmic reticulum Ca²⁺ sensor, STIM1, which redistributes to puncta near the plasma membrane and, in some manner, activates plasma membrane channels comprising Orai1, -2, and -3 subunits. We show here that 2-APB blocks puncta formation of fluorescently tagged STIM1 in HEK293 cells. Accordingly, 2-APB also inhibited SOCE and ICRAC-like currents in cells co-expressing STIM1 with the CRAC channel subunit, Orai1, with similar potency. However, 2-APB inhibited STIM1 puncta formation less well in cells co-expressing Orai1, indicating that the inhibitory effects of 2-APB are not solely dependent upon STIM1 reversal. Further, 2-APB only partially inhibited SOCE and current in cells co-expressing STIM1 and Orai2 and activated sustained currents in HEK293 cells expressing Orai3 and STIM1. Interestingly, the Orai3-dependent currents activated by 2-APB showed large outward currents at potentials greater than +50 mV. Finally, Orai3, and to a lesser extent Orai1, could be directly activated by 2-APB, independently of internal Ca²⁺ stores and STIM1. These data reveal novel and complex actions of 2-APB effects on SOCE that can be attributed to effects on both STIM1 as well as Orai channel subunits.
Language	English
Dates of publication	2008-0711
Size	p. 19265-19273.
Publishing place	American Society for Biochemistry and Molecular Biology
Document type	Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
Database	NAL-Catalogue (AGRICOLA)

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Article: Ca²⁺ influx and protein scaffolding via TRPC3 sustain PKCβ and ERK activation in B cells

Numaga, Takuro / Nishida, Motohiro / Kiyonaka, Shigeki / Kato, Kenta / Katano, Masahiro / Mori, Emiko / Kurosaki, Tomohiro / Inoue, Ryuji / Hikida, Masaki / Putney, James W. Jr / Mori, Yasuo

Journal of cell science. 2010 Mar. 15, v. 123, no. 6

2010

Abstract: Ca²⁺ signaling mediated by phospholipase C that produces inositol 1,4,5-trisphosphate [Ins(1,4,5)P₃] and diacylglycerol (DAG) controls lymphocyte activation. In contrast to store-operated Ca²⁺ entry activated by Ins(1,4,5)P₃-induced Ca²⁺ release from ... ...

Abstract	Ca²⁺ signaling mediated by phospholipase C that produces inositol 1,4,5-trisphosphate [Ins(1,4,5)P₃] and diacylglycerol (DAG) controls lymphocyte activation. In contrast to store-operated Ca²⁺ entry activated by Ins(1,4,5)P₃-induced Ca²⁺ release from endoplasmic reticulum, the importance of DAG-activated Ca²⁺ entry remains elusive. Here, we describe the physiological role of DAG-activated Ca²⁺ entry channels in B-cell receptor (BCR) signaling. In avian DT40 B cells, deficiency of transient receptor potential TRPC3 at the plasma membrane (PM) impaired DAG-activated cation currents and, upon BCR stimulation, the sustained translocation to the PM of protein kinase Cβ (PKCβ) that activated extracellular signal-regulated kinase (ERK). Notably, TRPC3 showed direct association with PKCβ that maintained localization of PKCβ at the PM. Thus, TRPC3 functions as both a Ca²⁺-permeable channel and a protein scaffold at the PM for downstream PKCβ activation in B cells.
Language	English
Dates of publication	2010-0315
Size	p. 927-938.
Publishing place	The Company of Biologists Limited
Document type	Article
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
Database	NAL-Catalogue (AGRICOLA)

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