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Article: Sorting nexins.

Carlton, Jez G / Cullen, Peter J

2005 Volume 15, Issue 20, Page(s) R819–20

MeSH term(s)	Binding Sites ; Carrier Proteins/metabolism ; Carrier Proteins/physiology ; Endosomes/metabolism ; Models, Biological ; Phosphatidylinositols/metabolism ; Protein Structure, Tertiary ; Protein Transport/physiology ; Sorting Nexins ; Vesicular Transport Proteins/metabolism ; Vesicular Transport Proteins/physiology
Chemical Substances	Carrier Proteins ; Phosphatidylinositols ; Sorting Nexins ; Vesicular Transport Proteins
Language	English
Publishing date	2005-10-25
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2005.10.012
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Article: Coincidence detection in phosphoinositide signaling.

Carlton, Jez G / Cullen, Peter J

Trends in cell biology

2005 Volume 15, Issue 10, Page(s) 540–547

Abstract: Phosphoinositide lipids function as both signaling molecules and as compartment-specific localization signals for phosphoinositide-binding proteins. In recent years, both phosphoinositides and phosphoinositide-binding proteins have been reported to ... ...

Abstract	Phosphoinositide lipids function as both signaling molecules and as compartment-specific localization signals for phosphoinositide-binding proteins. In recent years, both phosphoinositides and phosphoinositide-binding proteins have been reported to display a restricted, rather than a uniform, distribution across intracellular membranes. Here, we examine recent data documenting the restricted distribution of both phosphoinositides and phosphoinositide-binding proteins and examine how phosphoinositide-binding proteins might engage multiple binding partners to achieve these restricted localizations, effectively acting as detectors of coincident localization signals.
MeSH term(s)	Enzyme Activation ; Lipid Metabolism ; Lipids/chemistry ; Membrane Microdomains ; Models, Molecular ; Molecular Structure ; Phosphatidylinositols/chemistry ; Phosphatidylinositols/metabolism ; Second Messenger Systems/physiology
Chemical Substances	Lipids ; Phosphatidylinositols
Language	English
Publishing date	2005-08-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	30122-x
ISSN	1879-3088 ; 0962-8924
ISSN (online)	1879-3088
ISSN	0962-8924
DOI	10.1016/j.tcb.2005.08.005
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Article ; Online: Differential requirements for Alix and ESCRT-III in cytokinesis and HIV-1 release.

Carlton, Jez G / Agromayor, Monica / Martin-Serrano, Juan

Proceedings of the National Academy of Sciences of the United States of America

2008 Volume 105, Issue 30, Page(s) 10541–10546

Abstract: The ESCRT machinery functions in topologically equivalent membrane fission events, namely multivesicular body formation, the terminal stages of cytokinesis and HIV-1 release. Here, we show that the ESCRT-III-binding protein Alix is recruited to the ... ...

Abstract	The ESCRT machinery functions in topologically equivalent membrane fission events, namely multivesicular body formation, the terminal stages of cytokinesis and HIV-1 release. Here, we show that the ESCRT-III-binding protein Alix is recruited to the midbody of dividing cells through binding Cep55 via an evolutionarily conserved peptide. Disruption of Cep55/Alix/ESCRT-III interactions causes formation of aberrant midbodies and cytokinetic failure, demonstrating an essential role for these proteins in midbody morphology and cell division. We also show that the C terminus of Alix encodes a multimerization activity that is essential for its function in Alix-dependent HIV-1 release and for interaction with Tsg101. Last, we demonstrate that overexpression of Chmp4b and Chmp4c differentially inhibits HIV-1 release and cytokinesis, suggesting possible reasons for gene expansion within the mammalian Class E VPS pathway.
MeSH term(s)	Calcium-Binding Proteins/metabolism ; Cell Cycle Proteins/metabolism ; Cell Nucleus/metabolism ; Cytokinesis ; DNA-Binding Proteins/metabolism ; Endosomal Sorting Complexes Required for Transport ; Endosomes/metabolism ; Gene Expression Regulation ; Gene Expression Regulation, Viral ; HIV-1/metabolism ; HeLa Cells ; Humans ; Models, Biological ; Nuclear Proteins/metabolism ; Protein Binding ; Protein Structure, Tertiary ; RNA, Small Interfering/metabolism ; Transcription Factors/metabolism ; Vesicular Transport Proteins/metabolism
Chemical Substances	Calcium-Binding Proteins ; Cell Cycle Proteins ; Cep55 protein, human ; DNA-Binding Proteins ; Endosomal Sorting Complexes Required for Transport ; Nuclear Proteins ; PDCD6IP protein, human ; RNA, Small Interfering ; Transcription Factors ; Tsg101 protein ; Vesicular Transport Proteins
Language	English
Publishing date	2008-07-18
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.0802008105
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Article: Differential requirements for Alix and ESCRT-III in cytokinesis and HIV-1 release

Carlton, Jez G / Agromayor, Monica / Martin-Serrano, Juan

Proceedings of the National Academy of Sciences of the United States of America. 2008 July 29, v. 105, no. 30

2008

Abstract	The ESCRT machinery functions in topologically equivalent membrane fission events, namely multivesicular body formation, the terminal stages of cytokinesis and HIV-1 release. Here, we show that the ESCRT-III-binding protein Alix is recruited to the midbody of dividing cells through binding Cep55 via an evolutionarily conserved peptide. Disruption of Cep55/Alix/ESCRT-III interactions causes formation of aberrant midbodies and cytokinetic failure, demonstrating an essential role for these proteins in midbody morphology and cell division. We also show that the C terminus of Alix encodes a multimerization activity that is essential for its function in Alix-dependent HIV-1 release and for interaction with Tsg101. Last, we demonstrate that overexpression of Chmp4b and Chmp4c differentially inhibits HIV-1 release and cytokinesis, suggesting possible reasons for gene expansion within the mammalian Class E VPS pathway.
Language	English
Dates of publication	2008-0729
Size	p. 10541-10546.
Publishing place	National Academy of Sciences
Document type	Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
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Article ; Online: Parallels between cytokinesis and retroviral budding: a role for the ESCRT machinery.

Carlton, Jez G / Martin-Serrano, Juan

Science (New York, N.Y.)

2007 Volume 316, Issue 5833, Page(s) 1908–1912

Abstract: During cytokinesis, as dividing animal cells pull apart into two daughter cells, the final stage, termed abscission, requires breakage of the midbody, a thin membranous stalk connecting the daughter cells. This membrane fission event topologically ... ...

Abstract	During cytokinesis, as dividing animal cells pull apart into two daughter cells, the final stage, termed abscission, requires breakage of the midbody, a thin membranous stalk connecting the daughter cells. This membrane fission event topologically resembles the budding of viruses, such as HIV-1, from infected cells. We found that two proteins involved in HIV-1 budding-tumor susceptibility gene 101 (Tsg101), a subunit of the endosomal sorting complex required for transport I (ESCRT-I), and Alix, an ESCRT-associated protein-were recruited to the midbody during cytokinesis by interaction with centrosome protein 55 (Cep55), a centrosome and midbody protein essential for abscission. Tsg101, Alix, and possibly other components of ESCRT-I were required for the completion of cytokinesis. Thus, HIV-1 budding and cytokinesis use a similar subset of cellular components to carry out topologically similar membrane fission events.
MeSH term(s)	Adenosine Triphosphatases/metabolism ; Amino Acid Motifs ; Calcium-Binding Proteins/metabolism ; Carrier Proteins/metabolism ; Cell Cycle Proteins/metabolism ; Cytokinesis ; DNA-Binding Proteins/metabolism ; Endosomal Sorting Complexes Required for Transport ; Endosomes/metabolism ; HIV-1/physiology ; HeLa Cells ; Humans ; Microtubules/metabolism ; Nuclear Proteins/metabolism ; Protein Binding ; Protein Structure, Tertiary ; R-SNARE Proteins/metabolism ; RNA Interference ; Recombinant Fusion Proteins/metabolism ; Syntaxin 1/metabolism ; Transcription Factors/metabolism ; Transfection ; Vesicular Transport Proteins/metabolism
Chemical Substances	Calcium-Binding Proteins ; Carrier Proteins ; Cell Cycle Proteins ; Cep55 protein, human ; DNA-Binding Proteins ; Endosomal Sorting Complexes Required for Transport ; Nuclear Proteins ; PDCD6IP protein, human ; R-SNARE Proteins ; Recombinant Fusion Proteins ; STX2 protein, human ; Syntaxin 1 ; Transcription Factors ; Tsg101 protein ; VAMP8 protein, human ; Vesicular Transport Proteins ; Adenosine Triphosphatases (EC 3.6.1.-)
Language	English
Publishing date	2007-06-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.1143422
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Article: Parallels Between Cytokinesis and Retroviral Budding: A Role for the ESCRT Machinery

Carlton, Jez G / Martin-Serrano, Juan

Science. 2007 June 29, v. 316, no. 5833

2007

Abstract	During cytokinesis, as dividing animal cells pull apart into two daughter cells, the final stage, termed abscission, requires breakage of the midbody, a thin membranous stalk connecting the daughter cells. This membrane fission event topologically resembles the budding of viruses, such as HIV-1, from infected cells. We found that two proteins involved in HIV-1 budding--tumor susceptibility gene 101 (Tsg101), a subunit of the endosomal sorting complex required for transport I (ESCRT-I), and Alix, an ESCRT-associated protein--were recruited to the midbody during cytokinesis by interaction with centrosome protein 55 (Cep55), a centrosome and midbody protein essential for abscission. Tsg101, Alix, and possibly other components of ESCRT-I were required for the completion of cytokinesis. Thus, HIV-1 budding and cytokinesis use a similar subset of cellular components to carry out topologically similar membrane fission events.
Keywords	abscission ; centrosomes ; cytokinesis ; genes ; Human immunodeficiency virus 1 ; proteins ; viruses
Language	English
Dates of publication	2007-0629
Size	p. 1908-1912.
Publishing place	American Association for the Advancement of Science
Document type	Article
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.1143422
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Article ; Online: Essential role of hIST1 in cytokinesis.

Agromayor, Monica / Carlton, Jez G / Phelan, John P / Matthews, Daniel R / Carlin, Leo M / Ameer-Beg, Simon / Bowers, Katherine / Martin-Serrano, Juan

Molecular biology of the cell

2009 Volume 20, Issue 5, Page(s) 1374–1387

Abstract: The last steps of multivesicular body (MVB) formation, human immunodeficiency virus (HIV)-1 budding and cytokinesis require a functional endosomal sorting complex required for transport (ESCRT) machinery to facilitate topologically equivalent membrane ... ...

Abstract	The last steps of multivesicular body (MVB) formation, human immunodeficiency virus (HIV)-1 budding and cytokinesis require a functional endosomal sorting complex required for transport (ESCRT) machinery to facilitate topologically equivalent membrane fission events. Increased sodium tolerance (IST) 1, a new positive modulator of the ESCRT pathway, has been described recently, but an essential function of this highly conserved protein has not been identified. Here, we describe the previously uncharacterized KIAA0174 as the human homologue of IST1 (hIST1), and we report its conserved interaction with VPS4, CHMP1A/B, and LIP5. We also identify a microtubule interacting and transport (MIT) domain interacting motif (MIM) in hIST1 that is necessary for its interaction with VPS4, LIP5 and other MIT domain-containing proteins, namely, MITD1, AMSH, UBPY, and Spastin. Importantly, hIST1 is essential for cytokinesis in mammalian cells but not for HIV-1 budding, thus providing a novel mechanism of functional diversification of the ESCRT machinery. Last, we show that the hIST1 MIM activity is essential for cytokinesis, suggesting possible mechanisms to explain the role of hIST1 in the last step of mammalian cell division.
MeSH term(s)	Amino Acid Sequence ; Binding Sites ; Carrier Proteins/metabolism ; Cytokinesis/physiology ; Endosomal Sorting Complexes Required for Transport ; Endosomes/metabolism ; HIV-1/physiology ; HeLa Cells ; Humans ; Molecular Sequence Data ; Nuclear Proteins/metabolism ; Oncogene Proteins/analysis ; Oncogene Proteins/chemistry ; Oncogene Proteins/physiology ; Protein Interaction Mapping ; Protein Structure, Tertiary ; Protein Transport/genetics ; Sequence Alignment ; Vesicular Transport Proteins
Chemical Substances	CHMP1A protein, human ; Carrier Proteins ; Endosomal Sorting Complexes Required for Transport ; IST1 protein, human ; Nuclear Proteins ; Oncogene Proteins ; VTA1 protein, human ; Vesicular Transport Proteins
Language	English
Publishing date	2009-01-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E08-05-0474
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Article: SNX4 coordinates endosomal sorting of TfnR with dynein-mediated transport into the endocytic recycling compartment.

Traer, Colin J / Rutherford, Anna C / Palmer, Krysten J / Wassmer, Thomas / Oakley, Jacqueline / Attar, Naomi / Carlton, Jez G / Kremerskothen, Joachim / Stephens, David J / Cullen, Peter J

Nature cell biology

2007 Volume 9, Issue 12, Page(s) 1370–1380

Abstract: SNX-BAR proteins are a sub-family of sorting nexins implicated in endosomal sorting. Here, we establish that through its phox homology (PX) and Bin-Amphiphysin-Rvs (BAR) domains, sorting nexin-4 (SNX4) is associated with tubular and vesicular elements of ...

Abstract	SNX-BAR proteins are a sub-family of sorting nexins implicated in endosomal sorting. Here, we establish that through its phox homology (PX) and Bin-Amphiphysin-Rvs (BAR) domains, sorting nexin-4 (SNX4) is associated with tubular and vesicular elements of a compartment that overlaps with peripheral early endosomes and the juxtanuclear endocytic recycling compartment (ERC). Suppression of SNX4 perturbs transport between these compartments and causes lysosomal degradation of the transferrin receptor (TfnR). Through an interaction with KIBRA, a protein previously shown to bind dynein light chain 1, we establish that SNX4 associates with the minus end-directed microtubule motor dynein. Although suppression of KIBRA and dynein perturbs early endosome-to-ERC transport, TfnR sorting is maintained. We propose that by driving membrane tubulation, SNX4 coordinates iterative, geometric-based sorting of the TfnR with the long-range transport of carriers from early endosomes to the ERC. Finally, these data suggest that by associating with molecular motors, SNX-BAR proteins may coordinate sorting with carrier transport between donor and recipient membranes.
MeSH term(s)	Cell Compartmentation ; Cell Membrane/metabolism ; Dyneins/physiology ; Endocytosis ; Endosomes/metabolism ; HeLa Cells ; Humans ; Intracellular Signaling Peptides and Proteins ; Microtubules/metabolism ; Phosphoproteins ; Protein Binding ; Protein Transport ; Proteins/metabolism ; Receptors, Transferrin/metabolism ; Sorting Nexins ; Vesicular Transport Proteins/physiology
Chemical Substances	Intracellular Signaling Peptides and Proteins ; Phosphoproteins ; Proteins ; Receptors, Transferrin ; SNX4 protein, human ; Sorting Nexins ; Vesicular Transport Proteins ; WWC1 protein, human ; Dyneins (EC 3.6.4.2)
Language	English
Publishing date	2007-11-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1474722-4
ISSN	1476-4679 ; 1465-7392
ISSN (online)	1476-4679
ISSN	1465-7392
DOI	10.1038/ncb1656
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Article: Sorting nexin-2 is associated with tubular elements of the early endosome, but is not essential for retromer-mediated endosome-to-TGN transport.

Carlton, Jez G / Bujny, Miriam V / Peter, Brian J / Oorschot, Viola M J / Rutherford, Anna / Arkell, Rebecca S / Klumperman, Judith / McMahon, Harvey T / Cullen, Peter J

Journal of cell science

2005 Volume 118, Issue Pt 19, Page(s) 4527–4539

Abstract: Sorting nexins are a large family of phox-homology-domain-containing proteins that have been implicated in the control of endosomal sorting. Sorting nexin-1 is a component of the mammalian retromer complex that regulates retrieval of the cation- ... ...

Abstract	Sorting nexins are a large family of phox-homology-domain-containing proteins that have been implicated in the control of endosomal sorting. Sorting nexin-1 is a component of the mammalian retromer complex that regulates retrieval of the cation-independent mannose 6-phosphate receptor from endosomes to the trans-Golgi network. In yeast, retromer is composed of Vps5p (the orthologue of sorting nexin-1), Vps17p (a related sorting nexin) and a cargo selective subcomplex composed of Vps26p, Vps29p and Vps35p. With the exception of Vps17p, mammalian orthologues of all yeast retromer components have been identified. For Vps17p, one potential mammalian orthologue is sorting nexin-2. Here we show that, like sorting nexin-1, sorting nexin-2 binds phosphatidylinositol 3-monophosphate and phosphatidylinositol 3,5-bisphosphate, and possesses a Bin/Amphiphysin/Rvs domain that can sense membrane curvature. However, in contrast to sorting nexin-1, sorting nexin-2 could not induce membrane tubulation in vitro or in vivo. Functionally, we show that endogenous sorting nexin-1 and sorting nexin-2 co-localise on high curvature tubular elements of the 3-phosphoinositide-enriched early endosome, and that suppression of sorting nexin-2 does not perturb the degradative sorting of receptors for epidermal growth factor or transferrin, nor the steady-state distribution of the cation-independent mannose 6-phosphate receptor. However, suppression of sorting nexin-2 results in a subtle alteration in the kinetics of cation-independent mannose 6-phosphate receptor retrieval. These data suggest that although sorting nexin-2 may be a component of the retromer complex, its presence is not essential for the regulation of endosome-to-trans Golgi network retrieval of the cation-independent mannose 6-phosphate receptor.
MeSH term(s)	Animals ; Biological Transport/physiology ; Biomarkers ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Endosomes/metabolism ; Endosomes/ultrastructure ; ErbB Receptors/metabolism ; HeLa Cells ; Humans ; Lipid Bilayers/chemistry ; Lipid Bilayers/metabolism ; Liposomes/metabolism ; Phosphatidylinositol Phosphates/metabolism ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; RNA, Small Interfering/genetics ; RNA, Small Interfering/metabolism ; Receptor, IGF Type 2/metabolism ; Receptors, Transferrin/metabolism ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Vesicular Transport Proteins/genetics ; Vesicular Transport Proteins/metabolism ; trans-Golgi Network/metabolism ; trans-Golgi Network/ultrastructure
Chemical Substances	Biomarkers ; Carrier Proteins ; Lipid Bilayers ; Liposomes ; Phosphatidylinositol Phosphates ; Protein Isoforms ; RNA, Small Interfering ; Receptor, IGF Type 2 ; Receptors, Transferrin ; Recombinant Fusion Proteins ; Vesicular Transport Proteins ; phosphatidylinositol 3,5-diphosphate ; phosphatidylinositol 3-phosphate ; ErbB Receptors (EC 2.7.10.1)
Language	English
Publishing date	2005-09-18
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.02568
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Article: Sorting nexin-2 is associated with tubular elements of the early endosome, but is not essential for retromer-mediated endosome-to-TGN transport

Carlton, Jez G / Bujny, Miriam V / Peter, Brian J / Oorschot, Viola M. J / Rutherford, Anna / Arkell, Rebecca S / Klumperman, Judith / McMahon, Harvey T / Cullen, Peter J

Journal of cell science. 2005 Oct. 1, v. 118, no. 19

2005

Abstract	Sorting nexins are a large family of phox-homology-domain-containing proteins that have been implicated in the control of endosomal sorting. Sorting nexin-1 is a component of the mammalian retromer complex that regulates retrieval of the cation-independent mannose 6-phosphate receptor from endosomes to the trans-Golgi network. In yeast, retromer is composed of Vps5p (the orthologue of sorting nexin-1), Vps17p (a related sorting nexin) and a cargo selective subcomplex composed of Vps26p, Vps29p and Vps35p. With the exception of Vps17p, mammalian orthologues of all yeast retromer components have been identified. For Vps17p, one potential mammalian orthologue is sorting nexin-2. Here we show that, like sorting nexin-1, sorting nexin-2 binds phosphatidylinositol 3-monophosphate and phosphatidylinositol 3,5-bisphosphate, and possesses a Bin/Amphiphysin/Rvs domain that can sense membrane curvature. However, in contrast to sorting nexin-1, sorting nexin-2 could not induce membrane tubulation in vitro or in vivo. Functionally, we show that endogenous sorting nexin-1 and sorting nexin-2 co-localise on high curvature tubular elements of the 3-phosphoinositide-enriched early endosome, and that suppression of sorting nexin-2 does not perturb the degradative sorting of receptors for epidermal growth factor or transferrin, nor the steady-state distribution of the cation-independent mannose 6-phosphate receptor. However, suppression of sorting nexin-2 results in a subtle alteration in the kinetics of cation-independent mannose 6-phosphate receptor retrieval. These data suggest that although sorting nexin-2 may be a component of the retromer complex, its presence is not essential for the regulation of endosome-to-trans Golgi network retrieval of the cation-independent mannose 6-phosphate receptor.
Language	English
Dates of publication	2005-1001
Size	p. 4527-4539.
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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