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Article ; Online: An MBoC favorite: role of GTP hydrolysis in microtubule dynamics: information from a slowly hydrolyzable analogue, GMPCPP.

Chen, Chun-Ting / Doxsey, Stephen J

2013 Volume 23, Issue 19, Page(s) 3775

Language	English
Publishing date	2013-01-01
Publishing country	United States
Document type	Comment ; Journal Article
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E12-03-0186
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Zs.MO 410: Show issues

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Article: Molecular links between centrosome and midbody.

Doxsey, Stephen J

Molecular cell

2005 Volume 20, Issue 2, Page(s) 170–172

Abstract: The terminal step in cytokinesis that severs a cell in two-abscission-is poorly understood. In Developmental Cell, Fabbro et al (2005) identify a centrosome protein whose multiple phosphorylations regulate its movement from centrosome to midbody and ... ...

Abstract	The terminal step in cytokinesis that severs a cell in two-abscission-is poorly understood. In Developmental Cell, Fabbro et al (2005) identify a centrosome protein whose multiple phosphorylations regulate its movement from centrosome to midbody and completion of abscission.
MeSH term(s)	Animals ; Cell Cycle Proteins/metabolism ; Centrosome/metabolism ; Cytokinesis/physiology ; Cytoskeletal Proteins/metabolism ; Humans ; Models, Biological ; Nuclear Proteins/metabolism
Chemical Substances	CNTRL protein, human ; Cell Cycle Proteins ; Cep55 protein, human ; Cytoskeletal Proteins ; Nuclear Proteins
Language	English
Publishing date	2005-10-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2005.10.010
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Article ; Online: Pericentrin in cellular function and disease.

Delaval, Benedicte / Doxsey, Stephen J

The Journal of cell biology

2009 Volume 188, Issue 2, Page(s) 181–190

Abstract: Pericentrin is an integral component of the centrosome that serves as a multifunctional scaffold for anchoring numerous proteins and protein complexes. Through these interactions, pericentrin contributes to a diversity of fundamental cellular processes. ... ...

Abstract	Pericentrin is an integral component of the centrosome that serves as a multifunctional scaffold for anchoring numerous proteins and protein complexes. Through these interactions, pericentrin contributes to a diversity of fundamental cellular processes. Recent studies link pericentrin to a growing list of human disorders. Studies on pericentrin at the cellular, molecular, and, more recently, organismal level, provide a platform for generating models to elucidate the etiology of these disorders. Although the complexity of phenotypes associated with pericentrin-mediated disorders is somewhat daunting, insights into the cellular basis of disease are beginning to come into focus. In this review, we focus on human conditions associated with loss or elevation of pericentrin and propose cellular and molecular models that might explain them.
MeSH term(s)	Animals ; Antigens/genetics ; Antigens/metabolism ; Cell Death/genetics ; Centrosome/metabolism ; Centrosome/ultrastructure ; Dwarfism/genetics ; Genetic Predisposition to Disease/genetics ; Humans ; Mental Disorders/genetics ; Microtubules/genetics ; Microtubules/metabolism ; Mitosis/genetics ; Neoplasms/genetics ; Spindle Apparatus/genetics ; Spindle Apparatus/metabolism
Chemical Substances	Antigens ; pericentrin
Language	English
Publishing date	2009-12-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.200908114
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Article ; Online: New dimensions of asymmetric division in vertebrates.

Vertii, Anastassiia / Kaufman, Paul D / Hehnly, Heidi / Doxsey, Stephen

Cytoskeleton (Hoboken, N.J.)

2018 Volume 75, Issue 3, Page(s) 87–102

Abstract: Traditionally, we imagine that cell division gives rise to two identical daughter cells. Nevertheless, all cell divisions, to some degree, display asymmetry. Asymmetric cell division is defined as the generation of two daughter cells with different ... ...

Abstract	Traditionally, we imagine that cell division gives rise to two identical daughter cells. Nevertheless, all cell divisions, to some degree, display asymmetry. Asymmetric cell division is defined as the generation of two daughter cells with different physical content and/or developmental potential. Several organelles and cellular components including the centrosome, non-coding RNA, chromatin, and recycling endosomes are involved in the process of asymmetric cell division. Disruption of this important process is known to induce profound defects in development, the immune response, regeneration of tissues, aging, and cancer. Here, we discuss recent advances that expand our understanding of the mechanisms and consequences of asymmetric cell division in vertebrate organisms.
MeSH term(s)	Animals ; Asymmetric Cell Division ; Humans ; Mitosis ; Stem Cells/cytology ; Vertebrates
Language	English
Publishing date	2018-02-08
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2534372-5
ISSN	1949-3592 ; 1949-3584
ISSN (online)	1949-3592
ISSN	1949-3584
DOI	10.1002/cm.21434
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Article ; Online: Orchestrating vesicle transport, ESCRTs and kinase surveillance during abscission.

Chen, Chun-Ting / Hehnly, Heidi / Doxsey, Stephen J

Nature reviews. Molecular cell biology

2012 Volume 13, Issue 8, Page(s) 483–488

Abstract: During the final stage of cell division, the future daughter cells are physically separated through abscission. This process requires coordination of many molecular machines, including endocytic and secretory vesicle trafficking proteins as well as ESCRT ...

Abstract	During the final stage of cell division, the future daughter cells are physically separated through abscission. This process requires coordination of many molecular machines, including endocytic and secretory vesicle trafficking proteins as well as ESCRT (endosomal sorting complex required for transport) proteins, that mediate a complex series of events to culminate in the final separation of daughter cells. Abscission is coordinated with other cellular processes (for example, nuclear pore reassembly) through mitotic kinases such as Aurora B and Polo-like kinase 1, which act as master regulators to ensure proper progression of abscission.
MeSH term(s)	Animals ; Aurora Kinases ; Cell Cycle Proteins/metabolism ; Cell Division/physiology ; Cytokinesis/physiology ; Endosomal Sorting Complexes Required for Transport/metabolism ; Endosomes/physiology ; Nuclear Pore/physiology ; Protein Serine-Threonine Kinases/metabolism ; Protein Transport/physiology ; Proto-Oncogene Proteins/metabolism ; Signal Transduction ; Polo-Like Kinase 1
Chemical Substances	Cell Cycle Proteins ; Endosomal Sorting Complexes Required for Transport ; Proto-Oncogene Proteins ; Aurora Kinases (EC 2.7.11.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2012-07-11
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
ZDB-ID	2031313-5
ISSN	1471-0080 ; 1471-0072
ISSN (online)	1471-0080
ISSN	1471-0072
DOI	10.1038/nrm3395
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Zs.A 5446: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Resurrecting remnants: the lives of post-mitotic midbodies.

Chen, Chun-Ting / Ettinger, Andreas W / Huttner, Wieland B / Doxsey, Stephen J

Trends in cell biology

2012 Volume 23, Issue 3, Page(s) 118–128

Abstract: Around a century ago, the midbody (MB) was described as a structural assembly within the intercellular bridge during cytokinesis that served to connect the two future daughter cells. The MB has become the focus of intense investigation through the ... ...

Abstract	Around a century ago, the midbody (MB) was described as a structural assembly within the intercellular bridge during cytokinesis that served to connect the two future daughter cells. The MB has become the focus of intense investigation through the identification of a growing number of diverse cellular and molecular pathways that localize to the MB and contribute to its cytokinetic functions, ranging from selective vesicle trafficking and regulated microtubule (MT), actin, and endosomal sorting complex required for transport (ESCRT) filament assembly and disassembly to post-translational modification, such as ubiquitination. More recent studies have revealed new and unexpected functions of MBs in post-mitotic cells. In this review, we provide a historical perspective, discuss exciting new roles for MBs beyond their cytokinetic function, and speculate on their potential contributions to pluripotency.
MeSH term(s)	Actins/genetics ; Actins/metabolism ; Animals ; Autophagy/genetics ; Cytokinesis/genetics ; Endosomal Sorting Complexes Required for Transport/genetics ; Endosomal Sorting Complexes Required for Transport/metabolism ; HeLa Cells ; Humans ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Microtubules/genetics ; Microtubules/metabolism ; Pluripotent Stem Cells/cytology ; Pluripotent Stem Cells/metabolism ; Protein Processing, Post-Translational ; Protein Transport ; Ubiquitination
Chemical Substances	Actins ; Endosomal Sorting Complexes Required for Transport ; Intracellular Signaling Peptides and Proteins
Language	English
Publishing date	2012-12-11
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	30122-x
ISSN	1879-3088 ; 0962-8924
ISSN (online)	1879-3088
ISSN	0962-8924
DOI	10.1016/j.tcb.2012.10.012
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Article: Pericentrin in cellular function and disease

Delaval, Benedicte / Doxsey, Stephen J

Journal of cell biology. 2010, v. 188, no. 2

2010

Abstract	Pericentrin is an integral component of the centrosome that serves as a multifunctional scaffold for anchoring numerous proteins and protein complexes. Through these interactions, pericentrin contributes to a diversity of fundamental cellular processes. Recent studies link pericentrin to a growing list of human disorders. Studies on pericentrin at the cellular, molecular, and, more recently, organismal level, provide a platform for generating models to elucidate the etiology of these disorders. Although the complexity of phenotypes associated with pericentrin-mediated disorders is somewhat daunting, insights into the cellular basis of disease are beginning to come into focus. In this review, we focus on human conditions associated with loss or elevation of pericentrin and propose cellular and molecular models that might explain them.
Language	English
Size	p. 181-190.
Publishing place	The Rockefeller University Press
Document type	Article
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
Database	NAL-Catalogue (AGRICOLA)

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Article: Mutations and aneuploidy: co-conspirators in cancer?

Pihan, German / Doxsey, Stephen J

Cancer cell

2003 Volume 4, Issue 2, Page(s) 89–94

Abstract: The role of intragenic point mutations in human cancer is well established. However, the contribution of massive genomic changes collectively known as aneuploidy is less certain. Recent experimental work suggests that aneuploidy is required for sporadic ... ...

Abstract	The role of intragenic point mutations in human cancer is well established. However, the contribution of massive genomic changes collectively known as aneuploidy is less certain. Recent experimental work suggests that aneuploidy is required for sporadic carcinogenesis in mice and that it may collaborate with intragenic mutations during tumorigenesis. The genomic plasticity afforded by aneuploidy could facilitate emergence of protumorigenic gene dosage changes and accelerate accumulation of oncogenes and loss of tumor suppressor genes. These new findings force us to rethink the pathogenesis of carcinoma in ways that have significant implications for diagnosis and therapy.
MeSH term(s)	Aneuploidy ; Animals ; Chromosome Breakage/genetics ; Chromosome Segregation ; Gene Dosage ; Humans ; Mitosis ; Mutation/genetics ; Neoplasms/genetics ; Neoplasms/pathology ; Neoplasms/therapy
Language	English
Publishing date	2003-08-25
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	2078448-X
ISSN	1878-3686 ; 1535-6108
ISSN (online)	1878-3686
ISSN	1535-6108
DOI	10.1016/s1535-6108(03)00195-8
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Article: Resurrecting remnants: the lives of post-mitotic midbodies

Chen, Chun-Ting / Ettinger, Andreas W / Huttner, Wieland B / Doxsey, Stephen J

Trends in cell biology. 2013 Mar., v. 23, no. 3

2013

Abstract	Around a century ago, the midbody (MB) was described as a structural assembly within the intercellular bridge during cytokinesis that served to connect the two future daughter cells. The MB has become the focus of intense investigation through the identification of a growing number of diverse cellular and molecular pathways that localize to the MB and contribute to its cytokinetic functions, ranging from selective vesicle trafficking and regulated microtubule (MT), actin, and endosomal sorting complex required for transport (ESCRT) filament assembly and disassembly to post-translational modification, such as ubiquitination. More recent studies have revealed new and unexpected functions of MBs in post-mitotic cells. In this review, we provide a historical perspective, discuss exciting new roles for MBs beyond their cytokinetic function, and speculate on their potential contributions to pluripotency.
Keywords	actin ; cytokinesis ; microtubules ; physiological transport ; ubiquitination
Language	English
Dates of publication	2013-03
Size	p. 118-128.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	30122-x
ISSN	1879-3088 ; 0962-8924
ISSN (online)	1879-3088
ISSN	0962-8924
DOI	10.1016/j.tcb.2012.10.012
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Article ; Online: Characterization of the human NEK7 interactome suggests catalytic and regulatory properties distinct from those of NEK6.

de Souza, Edmarcia Elisa / Meirelles, Gabriela Vaz / Godoy, Bárbara Biatriz / Perez, Arina Marina / Smetana, Juliana Helena Costa / Doxsey, Stephen J / McComb, Mark E / Costello, Catherine E / Whelan, Stephen A / Kobarg, Jörg

Journal of proteome research

2014 Volume 13, Issue 9, Page(s) 4074–4090

Abstract: Human NEK7 is a regulator of cell division and plays an important role in growth and survival of mammalian cells. Human NEK6 and NEK7 are closely related, consisting of a conserved C-terminal catalytic domain and a nonconserved and disordered N-terminal ... ...

Abstract	Human NEK7 is a regulator of cell division and plays an important role in growth and survival of mammalian cells. Human NEK6 and NEK7 are closely related, consisting of a conserved C-terminal catalytic domain and a nonconserved and disordered N-terminal regulatory domain, crucial to mediate the interactions with their respective proteins. Here, in order to better understand NEK7 cellular functions, we characterize the NEK7 interactome by two screening approaches: one using a yeast two-hybrid system and the other based on immunoprecipitation followed by mass spectrometry analysis. These approaches led to the identification of 61 NEK7 interactors that contribute to a variety of biological processes, including cell division. Combining additional interaction and phosphorylation assays from yeast two-hybrid screens, we validated CC2D1A, TUBB2B, MNAT1, and NEK9 proteins as potential NEK7 interactors and substrates. Notably, endogenous RGS2, TUBB, MNAT1, NEK9, and PLEKHA8 localized with NEK7 at key sites throughout the cell cycle, especially during mitosis and cytokinesis. Furthermore, we obtained evidence that the closely related kinases NEK6 and NEK7 do not share common interactors, with the exception of NEK9, and display different modes of protein interaction, depending on their N- and C-terminal regions, in distinct fashions. In summary, our work shows for the first time a comprehensive NEK7 interactome that, combined with functional in vitro and in vivo assays, suggests that NEK7 is a multifunctional kinase acting in different cellular processes in concert with cell division signaling and independently of NEK6.
MeSH term(s)	Cell Cycle/physiology ; Humans ; Immunoprecipitation ; Mass Spectrometry ; NIMA-Related Kinases ; Protein Binding ; Protein Interaction Maps/physiology ; Protein-Serine-Threonine Kinases/chemistry ; Protein-Serine-Threonine Kinases/metabolism ; Proteomics ; Two-Hybrid System Techniques
Chemical Substances	NEK6 protein, human (EC 2.7.11.1) ; NEK7 protein, human (EC 2.7.11.1) ; NIMA-Related Kinases (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2014-08-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2078618-9
ISSN	1535-3907 ; 1535-3893
ISSN (online)	1535-3907
ISSN	1535-3893
DOI	10.1021/pr500437x
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