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Article: Lipid transfer and metabolism across the endolysosomal-mitochondrial boundary.

Daniele, Tiziana / Schiaffino, Maria Vittoria

2016 Volume 1861, Issue 8 Pt B, Page(s) 880–894

Abstract: Lysosomes and mitochondria occupy a central stage in the maintenance of cellular homeostasis, by playing complementary roles in nutrient sensing and energy metabolism. Specifically, these organelles function as signaling hubs that integrate environmental ...

Abstract	Lysosomes and mitochondria occupy a central stage in the maintenance of cellular homeostasis, by playing complementary roles in nutrient sensing and energy metabolism. Specifically, these organelles function as signaling hubs that integrate environmental and endogenous stimuli with specific metabolic responses. In particular, they control various lipid biosynthetic and degradative pipelines, either directly or indirectly, by regulating major cellular metabolic pathways, and by physical and functional connections established with each other and with other organelles. Membrane contact sites allow the exchange of ions and molecules between organelles, even without membrane fusion, and are privileged routes for lipid transfer among different membrane compartments. These inter-organellar connections typically involve the endoplasmic reticulum. Direct membrane contacts have now been described also between lysosomes, autophagosomes, lipid droplets, and mitochondria. This review focuses on these recently identified membrane contact sites, and on their role in lipid biosynthesis, exchange, turnover and catabolism. This article is part of a Special Issue entitled: The cellular lipid landscape edited by Tim P. Levine and Anant K. Menon.
MeSH term(s)	Animals ; Biological Transport ; Endoplasmic Reticulum/metabolism ; Endosomes/metabolism ; Homeostasis/physiology ; Humans ; Lipid Metabolism/physiology ; Lipids/chemistry ; Lysosomes/metabolism ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism
Chemical Substances	Lipids
Language	English
Publishing date	2016-08
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbalip.2016.02.001
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Article ; Online: Signaling pathways in melanosome biogenesis and pathology.

Schiaffino, Maria Vittoria

The international journal of biochemistry & cell biology

2010 Volume 42, Issue 7, Page(s) 1094–1104

Abstract: Melanosomes are the specialized intracellular organelles of pigment cells devoted to the synthesis, storage and transport of melanin pigments, which are responsible for most visible pigmentation in mammals and other vertebrates. As a direct consequence, ... ...

Abstract	Melanosomes are the specialized intracellular organelles of pigment cells devoted to the synthesis, storage and transport of melanin pigments, which are responsible for most visible pigmentation in mammals and other vertebrates. As a direct consequence, any genetic mutation resulting in alteration of melanosomal function, either because affecting pigment cell survival, migration and differentiation, or because interfering with melanosome biogenesis, transport and transfer to keratinocytes, is immediately translated into color variations of skin, fur, hair or eyes. Thus, over 100 genes and proteins have been identified as pigmentary determinants in mammals, providing us with a deep understanding of this biological system, which functions by using mechanisms and processes that have parallels in other tissues and organs. In particular, many genes implicated in melanosome biogenesis have been characterized, so that melanosomes represent an incredible source of information and a model for organelles belonging to the secretory pathway. Furthermore, the function of melanosomes can be associated with common physiological phenotypes, such as variation of pigmentation among individuals, and with rare pathological conditions, such as albinism, characterized by severe visual defects. Among the most relevant mechanisms operating in melanosome biogenesis are the signal transduction pathways mediated by two peculiar G protein-coupled receptors: the melanocortin-1 receptor (MC1R), involved in the fair skin/red hair phenotype and skin cancer; and OA1 (GPR143), whose loss-of-function results in X-linked ocular albinism. This review will focus on the most recent novelties regarding the functioning of these two receptors, by highlighting emerging signaling mechanisms and general implications for cell biology and pathology.
MeSH term(s)	Albinism, Ocular/metabolism ; Albinism, Ocular/pathology ; Animals ; Eye Proteins/metabolism ; Humans ; Melanosomes/metabolism ; Melanosomes/pathology ; Melanosomes/ultrastructure ; Membrane Glycoproteins/metabolism ; Receptor, Melanocortin, Type 1/metabolism ; Signal Transduction ; Skin Neoplasms/metabolism ; Skin Neoplasms/pathology
Chemical Substances	Eye Proteins ; GPR143 protein, human ; Membrane Glycoproteins ; Receptor, Melanocortin, Type 1
Language	English
Publishing date	2010-04-08
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1228429-4
ISSN	1878-5875 ; 1357-2725
ISSN (online)	1878-5875
ISSN	1357-2725
DOI	10.1016/j.biocel.2010.03.023
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Article: Organelle biogenesis and interorganellar connections: Better in contact than in isolation.

Daniele, Tiziana / Schiaffino, Maria Vittoria

Communicative & integrative biology

2014 Volume 7, Page(s) e29587

Abstract: Membrane contact sites (MCSs) allow the exchange of molecules and information between organelles, even when their membranes cannot fuse directly. In recent years, a number of functions have been attributed to these contacts, highlighting their critical ... ...

Abstract	Membrane contact sites (MCSs) allow the exchange of molecules and information between organelles, even when their membranes cannot fuse directly. In recent years, a number of functions have been attributed to these contacts, highlighting their critical role in cell homeostasis. Although inter-organellar connections typically involve the endoplasmic reticulum (ER), we recently reported the presence of a novel MCSs between melanosomes and mitochondria. Melanosome-mitochondrion contacts appear mediated by fibrillar bridges resembling the protein tethers linking mitochondria and the ER, both for their ultrastructural features and the involvement of Mitofusin 2. The frequency of these connections correlates spatially and timely with melanosome biogenesis, suggesting a functional link between the 2 processes and in general that organelle biogenesis in the secretory pathway requires interorganellar crosstalks at multiple steps. Here, we summarize the different functions attributed to MCSs, and discuss their possible relevance for the newly identified melanosome-mitochondrion liaison.
Language	English
Publishing date	2014-06-23
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2451097-X
ISSN	1942-0889
ISSN	1942-0889
DOI	10.4161/cib.29587
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Article ; Online: Amino acid deprivation triggers a novel GCN2-independent response leading to the transcriptional reactivation of non-native DNA sequences.

De Vito, Annarosaria / Lazzaro, Massimo / Palmisano, Ilaria / Cittaro, Davide / Riba, Michela / Lazarevic, Dejan / Bannai, Makoto / Gabellini, Davide / Schiaffino, Maria Vittoria

PloS one

2018 Volume 13, Issue 7, Page(s) e0200783

Abstract: In a variety of species, reduced food intake, and in particular protein or amino acid (AA) restriction, extends lifespan and healthspan. However, the underlying epigenetic and/or transcriptional mechanisms are largely unknown, and dissection of specific ... ...

Abstract	In a variety of species, reduced food intake, and in particular protein or amino acid (AA) restriction, extends lifespan and healthspan. However, the underlying epigenetic and/or transcriptional mechanisms are largely unknown, and dissection of specific pathways in cultured cells may contribute to filling this gap. We have previously shown that, in mammalian cells, deprivation of essential AAs (methionine/cysteine or tyrosine) leads to the transcriptional reactivation of integrated silenced transgenes, including plasmid and retroviral vectors and latent HIV-1 provirus, by a process involving epigenetic chromatic remodeling and histone acetylation. Here we show that the deprivation of methionine/cysteine also leads to the transcriptional upregulation of endogenous retroviruses, suggesting that essential AA starvation affects the expression not only of exogenous non-native DNA sequences, but also of endogenous anciently-integrated and silenced parasitic elements of the genome. Moreover, we show that the transgene reactivation response is highly conserved in different mammalian cell types, and it is reproducible with deprivation of most essential AAs. The General Control Non-derepressible 2 (GCN2) kinase and the downstream integrated stress response represent the best candidates mediating this process; however, by pharmacological approaches, RNA interference and genomic editing, we demonstrate that they are not implicated. Instead, the response requires MEK/ERK and/or JNK activity and is reproduced by ribosomal inhibitors, suggesting that it is triggered by a novel nutrient-sensing and signaling pathway, initiated by translational block at the ribosome, and independent of mTOR and GCN2. Overall, these findings point to a general transcriptional response to essential AA deprivation, which affects the expression of non-native genomic sequences, with relevant implications for the epigenetic/transcriptional effects of AA restriction in health and disease.
MeSH term(s)	Amino Acids, Essential/deficiency ; Amino Acids, Essential/metabolism ; Animals ; Blotting, Western ; CRISPR-Cas Systems ; Cell Line ; Gene Editing ; HeLa Cells ; Hep G2 Cells ; Humans ; Mice ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; RNA Interference ; Real-Time Polymerase Chain Reaction ; Signal Transduction/genetics ; Signal Transduction/physiology ; Transcriptional Activation/genetics ; Transcriptional Activation/physiology
Chemical Substances	Amino Acids, Essential ; EIF2AK4 protein, human (EC 2.7.11.1) ; Eif2ak4 protein, mouse (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2018-07-18
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0200783
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Article: Passport control for foreign integrated DNAs: An unexpected checkpoint by class II HDAC4 revealed by amino acid starvation.

Palmisano, Ilaria / Della Chiara, Giulia / Schiaffino, Maria Vittoria / Poli, Guido

Mobile genetic elements

2013 Volume 2, Issue 5, Page(s) 233–238

Abstract: The endless battle between mammalian host cells and microbes has evolved mechanisms to shut down the expression of exogenous transcriptional units integrated into the genome with the goal of limiting their spreading. Recently, we observed that ... ...

Abstract	The endless battle between mammalian host cells and microbes has evolved mechanisms to shut down the expression of exogenous transcriptional units integrated into the genome with the goal of limiting their spreading. Recently, we observed that deprivation of essential amino acids leads to a selective, reversible upregulation of expression of exogenous transgenes, either carried by integrated plasmids or retroviral vectors, but not of their endogenous counterparts. This effect was dependent on epigenetic modifications and was mediated by the downregulation of the class II histone deacetylase-4 (HDAC4). Indeed, HDAC4 expression inversely correlated with that of the transgene and its inhibition or downregulation enhanced transgene expression. Could this be true also for "naturally" integrated proviruses? We investigated this question in the case of HIV-1, the etiological agent of AIDS and we observed that both amino acid starvation and HDAC4 inhibition triggered HIV-1 reactivation in chronically infected ACH-2 T lymphocytic cells (HDAC4
Language	English
Publishing date	2013-04-02
Publishing country	United States
Document type	Journal Article
ZDB-ID	2682444-9
ISSN	2159-256X ; 2159-2543
ISSN (online)	2159-256X
ISSN	2159-2543
DOI	10.4161/mge.22610
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Article ; Online: Mitochondria and melanosomes establish physical contacts modulated by Mfn2 and involved in organelle biogenesis.

Daniele, Tiziana / Hurbain, Ilse / Vago, Riccardo / Casari, Giorgio / Raposo, Graça / Tacchetti, Carlo / Schiaffino, Maria Vittoria

Current biology : CB

2014 Volume 24, Issue 4, Page(s) 393–403

Abstract: Background: To efficiently supply ATP to sites of high-energy demand and finely regulate calcium signaling, mitochondria adapt their metabolism, shape, and distribution within the cells, including relative positioning with respect to other organelles. ... ...

Abstract	Background: To efficiently supply ATP to sites of high-energy demand and finely regulate calcium signaling, mitochondria adapt their metabolism, shape, and distribution within the cells, including relative positioning with respect to other organelles. However, physical contacts between mitochondria and the secretory/endocytic pathway have been demonstrated so far only with the ER, through structural and functional interorganellar connections. Results: Here we show by electron tomography that mitochondria physically contact melanosomes, specialized lysosome-related organelles of pigment cells, through fibrillar bridges resembling the protein tethers linking mitochondria and the ER. Mitofusin (Mfn) 2, which bridges ER to mitochondria, specifically localizes also to melanosome-mitochondrion contacts, and its knockdown significantly reduces the interorganellar connections. Contacts are associated to the melanogenesis process, as indicated by the fact that they are reduced in a model of aberrant melanogenesis whereas they are enhanced both where melanosome biogenesis takes place in the perinuclear area and when it is actively stimulated by OA1, a G protein-coupled receptor implicated in ocular albinism and organellogenesis. Consistently, Mfn2 knockdown prevents melanogenesis activation by OA1, and the pharmacological inhibition of mitochondrial ATP synthesis severely reduces contact formation and impairs melanosome biogenesis, by affecting in particular the developing organelles showing the highest frequency of contacts. Conclusions: Altogether, our findings reveal the presence of an unprecedented physical and functional connection between mitochondria and the secretory/endocytic pathway that goes beyond the ER-mitochondria linkage and is spatially and timely associated to secretory organelle biogenesis.
MeSH term(s)	Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum/ultrastructure ; Golgi Apparatus/metabolism ; Golgi Apparatus/ultrastructure ; Melanosomes/metabolism ; Melanosomes/ultrastructure ; Membrane Proteins/metabolism ; Microscopy, Electron ; Mitochondria/metabolism ; Mitochondria/ultrastructure ; Organelles/metabolism ; Organelles/ultrastructure
Chemical Substances	Membrane Proteins
Language	English
Publishing date	2014-01-30
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2014.01.007
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Article ; Online: Melanosome-autonomous regulation of size and number: the OA1 receptor sustains PMEL expression.

Falletta, Paola / Bagnato, Paola / Bono, Maria / Monticone, Massimiliano / Schiaffino, Maria Vittoria / Bennett, Dorothy C / Goding, Colin R / Tacchetti, Carlo / Valetti, Caterina

Pigment cell & melanoma research

2014 Volume 27, Issue 4, Page(s) 565–579

Abstract: Little is known as to how cells ensure that organelle size and number are coordinated to correctly couple organelle biogenesis to the demands of proliferation or differentiation. OA1 is a melanosome-associated G-protein-coupled receptor involved in ... ...

Abstract	Little is known as to how cells ensure that organelle size and number are coordinated to correctly couple organelle biogenesis to the demands of proliferation or differentiation. OA1 is a melanosome-associated G-protein-coupled receptor involved in melanosome biogenesis during melanocyte differentiation. Cells lacking OA1 contain fewer, but larger, mature melanosomes. Here, we show that OA1 loss of function reduces both the basal expression and the α-melanocyte-stimulating hormone/cAMP-dependent induction of the microphthalmia-associated transcription factor (MITF), the master regulator of melanocyte differentiation. In turn, this leads to a significant reduction in expression of PMEL, a major melanosomal structural protein, but does not affect tyrosinase and melanin levels. In line with its pivotal role in sensing melanosome maturation, OA1 expression rescues melanosome biogenesis, activates MITF expression and thereby coordinates melanosome size and number, providing a quality control mechanism for the organelle in which resides. Thus, resident sensor receptors can activate a transcriptional cascade to specifically promote organelle biogenesis.
MeSH term(s)	Animals ; Base Sequence ; Cell Differentiation/physiology ; Cell Line ; Eye Proteins/genetics ; Eye Proteins/metabolism ; Gene Expression Regulation/physiology ; Humans ; Melanocytes/cytology ; Melanocytes/metabolism ; Melanosomes ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/metabolism ; Mice ; Mice, Knockout ; Microphthalmia-Associated Transcription Factor/genetics ; Microphthalmia-Associated Transcription Factor/metabolism ; Molecular Sequence Data ; Receptors, G-Protein-Coupled/genetics ; Receptors, G-Protein-Coupled/metabolism ; alpha-MSH/genetics ; alpha-MSH/metabolism ; gp100 Melanoma Antigen/biosynthesis ; gp100 Melanoma Antigen/genetics
Chemical Substances	Eye Proteins ; GPR143 protein, human ; Gpr143 protein, mouse ; MITF protein, human ; Membrane Glycoproteins ; Microphthalmia-Associated Transcription Factor ; Mitf protein, mouse ; PMEL protein, human ; Receptors, G-Protein-Coupled ; gp100 Melanoma Antigen ; alpha-MSH (581-05-5)
Language	English
Publishing date	2014-04-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2409570-9
ISSN	1755-148X ; 1600-0749 ; 0893-5785 ; 1755-1471
ISSN (online)	1755-148X ; 1600-0749
ISSN	0893-5785 ; 1755-1471
DOI	10.1111/pcmr.12239
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Article ; Online: Expression of OA1 limits the fusion of a subset of MVBs with lysosomes - a mechanism potentially involved in the initial biogenesis of melanosomes.

Burgoyne, Thomas / Jolly, Rushee / Martin-Martin, Belen / Seabra, Miguel C / Piccirillo, Rosanna / Schiaffino, Maria Vittoria / Futter, Clare E

Journal of cell science

2013 Volume 126, Issue Pt 22, Page(s) 5143–5152

Abstract: Multivesicular endosomes/bodies (MVBs) deliver proteins, such as activated EGF receptor (EGFR), to the lysosome for degradation, and, in pigmented cells, MVBs containing PMEL are an initial stage in melanosome biogenesis. The mechanisms regulating ... ...

Abstract	Multivesicular endosomes/bodies (MVBs) deliver proteins, such as activated EGF receptor (EGFR), to the lysosome for degradation, and, in pigmented cells, MVBs containing PMEL are an initial stage in melanosome biogenesis. The mechanisms regulating numbers and fate of different populations of MVB are unclear. Here, we focus on the role of the G-protein-coupled receptor OA1 (also known as GPR143), which is expressed exclusively in pigmented cells and mutations in which cause the most common type of ocular albinism. When exogenously expressing PMEL, HeLa cells have been shown to form MVBs resembling early stage melanosomes. To focus on the role of OA1 in the initial stages of melanosome biogenesis we take advantage of the absence of the later stages of melanosome maturation in HeLa cells to determine whether OA1 activity can regulate MVB number and fate. Expression of wild-type but not OA1 mutants carrying inactivating mutations or deletions causes MVB numbers to increase. Whereas OA1 expression has no effect on delivery of EGFR-containing MVBs to the lysosome, it inhibits the lysosomal delivery of PMEL and PMEL-containing MVBs accumulate. We propose that OA1 activity delays delivery of PMEL-containing MVBs to the lysosome to allow time for melanin synthesis and commitment to melanosome biogenesis.
MeSH term(s)	Endosomes/metabolism ; ErbB Receptors/genetics ; ErbB Receptors/metabolism ; Eye Proteins/biosynthesis ; Eye Proteins/genetics ; Gene Expression Regulation, Developmental ; HeLa Cells ; Humans ; Lysosomes/genetics ; Lysosomes/metabolism ; Melanosomes/genetics ; Melanosomes/metabolism ; Membrane Glycoproteins/biosynthesis ; Membrane Glycoproteins/genetics ; Multivesicular Bodies/genetics ; Multivesicular Bodies/metabolism ; Mutation ; gp100 Melanoma Antigen/metabolism
Chemical Substances	Eye Proteins ; GPR143 protein, human ; Membrane Glycoproteins ; PMEL protein, human ; gp100 Melanoma Antigen ; EGFR protein, human (EC 2.7.10.1) ; ErbB Receptors (EC 2.7.10.1)
Language	English
Publishing date	2013-09-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.128561
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Article ; Online: The ocular albinism type 1 protein, an intracellular G protein-coupled receptor, regulates melanosome transport in pigment cells.

Palmisano, Ilaria / Bagnato, Paola / Palmigiano, Angela / Innamorati, Giulio / Rotondo, Giuseppe / Altimare, Domenico / Venturi, Consuelo / Sviderskaya, Elena V / Piccirillo, Rosanna / Coppola, Massimiliano / Marigo, Valeria / Incerti, Barbara / Ballabio, Andrea / Surace, Enrico M / Tacchetti, Carlo / Bennett, Dorothy C / Schiaffino, Maria Vittoria

Human molecular genetics

2017 Volume 26, Issue 15, Page(s) 3028–3029

Language	English
Publishing date	2017-08-01
Publishing country	England
Document type	Journal Article
ZDB-ID	1108742-0
ISSN	1460-2083 ; 0964-6906
ISSN (online)	1460-2083
ISSN	0964-6906
DOI	10.1093/hmg/ddx131
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Article: An unconventional dileucine-based motif and a novel cytosolic motif are required for the lysosomal and melanosomal targeting of OA1

Piccirillo, Rosanna / Palmisano, Ilaria / Innamorati, Giulio / Bagnato, Paola / Altimare, Domenico / Schiaffino, Maria Vittoria

Journal of cell science. 2006 May 15, v. 119, no. 10

2006

Abstract: The protein product of the gene responsible for ocular albinism type 1, named OA1, is a pigment-cell-specific membrane glycoprotein, displaying features of G-protein-coupled receptors, yet exclusively localized to late endosomes, lysosomes and ... ...

Abstract	The protein product of the gene responsible for ocular albinism type 1, named OA1, is a pigment-cell-specific membrane glycoprotein, displaying features of G-protein-coupled receptors, yet exclusively localized to late endosomes, lysosomes and melanosomes. To dissect the signals responsible for the intracellular localization of OA1, we generated chimeric proteins consisting of the cytosolic domains of OA1 fused to the lumenal and transmembrane domains of LAMP1; in addition, we generated missense and deletion mutants of full-length OA1. Using this approach, we identified two separate sorting signals that are both necessary and sufficient for intracellular retention, as well as lysosomal and melanosomal localization, in melanocytic and non-melanocytic cells. These sorting signals are an unconventional dileucine motif within the third cytosolic loop and a novel motif, characterized by a tryptophan-glutamic acid doublet, within the C-terminal tail. Both motifs must be mutated to promote the plasma membrane localization of OA1, suggesting that they can independently drive its intracellular targeting. In addition, both motifs act similarly as lysosomal sorting signals in non-melanocytic cells, but appear to carry different specificities in melanocytic cells. Our findings indicate that OA1 contains multiple unconventional signals responsible for its lysosomal and melanosomal localization, and reveal a remarkable and unforeseen complexity in the regulation of polytopic protein sorting to specialized secretory organelles.
Language	English
Dates of publication	2006-0515
Size	p. 2003-2014.
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
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