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Article ; Online: WISp39 and Hsp90: actin' together in cell migration.

Fotedar, Rati / Margolis, Robert L

2015 Volume 6, Issue 20, Page(s) 17871–17872

MeSH term(s)	Actin Cytoskeleton/metabolism ; Actins/metabolism ; Animals ; Cell Movement ; HSP90 Heat-Shock Proteins/metabolism ; Humans ; Immunophilins/metabolism ; Protein Binding ; Signal Transduction
Chemical Substances	Actins ; FKBPL protein, human ; HSP90 Heat-Shock Proteins ; Immunophilins (EC 5.2.1.8)
Language	English
Publishing date	2015-07-20
Publishing country	United States
Document type	Editorial
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.4934
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Article ; Online: Obituary

Margolis Robert L / Fotedar Rati

Cell Division, Vol 2, Iss 1, p

Arun Fotedar

2007 Volume 29

Keywords	Cytology ; QH573-671 ; Biology (General) ; QH301-705.5 ; Science ; Q ; DOAJ:Cytology ; DOAJ:Biology ; DOAJ:Biology and Life Sciences
Language	English
Publishing date	2007-10-01T00:00:00Z
Publisher	BioMed Central
Document type	Article ; Online
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Article ; Online: Obituary: arun fotedar.

Fotedar, Rati / Margolis, Robert L

Cell division

2007 Volume 2, Page(s) 29

Language	English
Publishing date	2007-10-02
Publishing country	England
Document type	Editorial
ISSN	1747-1028
ISSN (online)	1747-1028
DOI	10.1186/1747-1028-2-29
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Article ; Online: Glioblastoma motility occurs in the absence of actin polymer.

Panopoulos, Andreas / Howell, Michael / Fotedar, Rati / Margolis, Robert L

Molecular biology of the cell

2011 Volume 22, Issue 13, Page(s) 2212–2220

Abstract: In fibroblasts and keratocytes, motility is actin dependent, while microtubules play a secondary role, providing directional guidance. We demonstrate here that the motility of glioblastoma cells is exceptional, in that it occurs in cells depleted of ... ...

Abstract	In fibroblasts and keratocytes, motility is actin dependent, while microtubules play a secondary role, providing directional guidance. We demonstrate here that the motility of glioblastoma cells is exceptional, in that it occurs in cells depleted of assembled actin. Cells display persistent motility in the presence of actin inhibitors at concentrations sufficient to fully disassemble actin. Such actin independent motility is characterized by the extension of cell protrusions containing abundant microtubule polymers. Strikingly, glioblastoma cells exhibit no motility in the presence of microtubule inhibitors, at concentrations that disassemble labile microtubule polymers. In accord with an unconventional mode of motility, glioblastoma cells have some unusual requirements for the Rho GTPases. While Rac1 is required for lamellipodial protrusions in fibroblasts, expression of dominant negative Rac1 does not suppress glioblastoma migration. Other GTPase mutants are largely without unique effect, except dominant positive Rac1-Q61L, and rapidly cycling Rac1-F28L, which substantially suppress glioblastoma motility. We conclude that glioblastoma cells display an unprecedented mode of intrinsic motility that can occur in the absence of actin polymer, and that appears to require polymerized microtubules.
MeSH term(s)	Actins/metabolism ; Cell Movement/physiology ; Fibroblasts/metabolism ; Glioblastoma/metabolism ; Glioblastoma/pathology ; Humans ; Microtubules/metabolism ; Mutation ; Polymerization ; Pseudopodia/metabolism ; Tumor Cells, Cultured ; rac1 GTP-Binding Protein/metabolism ; rho GTP-Binding Proteins/metabolism
Chemical Substances	Actins ; rac1 GTP-Binding Protein (EC 3.6.5.2) ; rho GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2011-05-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E10-10-0849
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Article ; Online: TD-60 is required for interphase cell cycle progression.

Yenjerla, Mythili / Panopoulos, Andreas / Reynaud, Caroline / Fotedar, Rati / Margolis, Robert L

Cell cycle (Georgetown, Tex.)

2013 Volume 12, Issue 5, Page(s) 837–841

Abstract: We previously identified TD-60 (RCC2) as a mitotic centromere-associated protein that is necessary for proper completion of mitosis. We now report that TD-60 is an essential regulator of cell cycle progression during interphase. siRNA suppression blocks ... ...

Abstract	We previously identified TD-60 (RCC2) as a mitotic centromere-associated protein that is necessary for proper completion of mitosis. We now report that TD-60 is an essential regulator of cell cycle progression during interphase. siRNA suppression blocks progression of mammalian G₁/S phase cells and progression of G₂ cells into mitosis. Prolonged arrest occurs both in non-transformed cells and in transformed cells lacking functional p53. TD-60 associates with Rac1 and Arf6 and has recently been demonstrated to be an element of α5β1 integrin and cortactin interactomes. These associations with known elements of cell cycle control, together with our data, suggest that TD-60 is an essential component of one or more signaling pathways that drive cell cycle progression. During mitosis, TD-60 is required for correct assembly of the mitotic spindle and activation of key mitotic proteins. In contrast, in interphase TD-60 promotes cell cycle progression through what must be distinct mechanisms. TD-60 thus appears to be one of the growing categories of proteins that "moonlight," or have more than one distinct cellular function.
MeSH term(s)	Chromosomal Proteins, Non-Histone/metabolism ; Gene Knockdown Techniques ; Guanine Nucleotide Exchange Factors/metabolism ; HeLa Cells ; Humans ; Interphase ; Mitosis ; RNA, Small Interfering/metabolism ; Transfection
Chemical Substances	Chromosomal Proteins, Non-Histone ; Guanine Nucleotide Exchange Factors ; RCC2 protein, human ; RNA, Small Interfering
Language	English
Publishing date	2013-02-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2146183-1
ISSN	1551-4005 ; 1538-4101 ; 1554-8627
ISSN (online)	1551-4005
ISSN	1538-4101 ; 1554-8627
DOI	10.4161/cc.23821
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Article ; Online: Substrate degradation by the anaphase promoting complex occurs during mitotic slippage.

Lee, Jinho / Kim, Jin Ah / Margolis, Robert L / Fotedar, Rati

Cell cycle (Georgetown, Tex.)

2010 Volume 9, Issue 9, Page(s) 1792–1801

Abstract: Microtubule targeting drugs are successful in chemotherapy because they indefinitely activate the spindle assembly checkpoint. The spindle assembly checkpoint monitors proper attachment of all kinetochores to microtubules and tension between the ... ...

Abstract	Microtubule targeting drugs are successful in chemotherapy because they indefinitely activate the spindle assembly checkpoint. The spindle assembly checkpoint monitors proper attachment of all kinetochores to microtubules and tension between the kinetochores of sister chromatids to prevent premature anaphase entry. To this end, the activated spindle assembly checkpoint suppresses the E3 ubiquitin ligase activity of the anaphase-promoting complex (APC). In the continued presence of conditions that activate the spindle assembly checkpoint, cells eventually escape from mitosis by "slippage". It has not been directly tested whether APC activation accompanies slippage. Using cells blocked in mitosis with the microtubule assembly inhibitor nocodazole, we show that mitotic APC substrates are degraded upon mitotic slippage. To confirm that APC is normally activated upon mitotic slippage we have found that knockdown of Cdc20 and Cdh1, two mitotic activators of APC, prevents the degradation of APC substrates during mitotic slippage. We provide the first direct demonstration that despite conditions that activate the spindle checkpoint, APC is indeed activated upon mitotic slippage of cells to interphase cells. Activation of the spindle checkpoint by microtubule targeting drugs used in chemotherapy may not indefinitely prevent APC activation.
MeSH term(s)	Anaphase-Promoting Complex-Cyclosome ; Antigens, CD ; Antineoplastic Agents/pharmacology ; Cadherins/genetics ; Cadherins/metabolism ; Cdc20 Proteins ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; G1 Phase ; Gene Knockdown Techniques ; HCT116 Cells ; Humans ; Mitosis ; Nocodazole/pharmacology ; S Phase ; Spindle Apparatus/metabolism ; Substrate Specificity ; Ubiquitin-Protein Ligase Complexes/metabolism ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	Antigens, CD ; Antineoplastic Agents ; CDH1 protein, human ; Cadherins ; Cdc20 Proteins ; Cell Cycle Proteins ; CDC20 protein, human (156288-95-8) ; Ubiquitin-Protein Ligase Complexes (EC 2.3.2.23) ; Anaphase-Promoting Complex-Cyclosome (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Nocodazole (SH1WY3R615)
Language	English
Publishing date	2010-05-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2146183-1
ISSN	1551-4005 ; 1538-4101 ; 1554-8627
ISSN (online)	1551-4005
ISSN	1538-4101 ; 1554-8627
DOI	10.4161/cc.9.9.11519
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Article ; Online: N-methyl-N'-nitro-N-nitrosoguanidine (MNNG) triggers MSH2 and Cdt2 protein-dependent degradation of the cell cycle and mismatch repair (MMR) inhibitor protein p21Waf1/Cip1.

Jascur, Thomas / Fotedar, Rati / Greene, Serena / Hotchkiss, Erin / Boland, C Richard

The Journal of biological chemistry

2011 Volume 286, Issue 34, Page(s) 29531–29539

Abstract: p21(Waf1/Cip1) protein levels respond to DNA damage; p21 is induced after ionizing radiation, but degraded after UV. p21 degradation after UV is necessary for optimal DNA repair, presumably because p21 inhibits nucleotide excision repair by blocking ... ...

Abstract	p21(Waf1/Cip1) protein levels respond to DNA damage; p21 is induced after ionizing radiation, but degraded after UV. p21 degradation after UV is necessary for optimal DNA repair, presumably because p21 inhibits nucleotide excision repair by blocking proliferating cell nuclear antigen (PCNA). Because p21 also inhibits DNA mismatch repair (MMR), we investigated how p21 levels respond to DNA alkylation by N-methyl-N'-nitro-N-nitrosoguanidine (MNNG), which triggers the MMR system. We show that MNNG caused rapid degradation of p21, and this involved the ubiquitin ligase Cdt2 and the proteasome. p21 degradation further required MSH2 but not MLH1. p21 mutants that cannot bind PCNA or cannot be ubiquitinated were resistant to MNNG. MNNG induced the formation of PCNA complexes with MSH6 and Cdt2. Finally, when p21 degradation was blocked, MNNG treatment resulted in reduced recruitment of MMR proteins to chromatin. This study describes a novel pathway that removes p21 to allow cells to efficiently activate the MMR system.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Chromatin/genetics ; Chromatin/metabolism ; Cyclin-Dependent Kinase Inhibitor p21/genetics ; Cyclin-Dependent Kinase Inhibitor p21/metabolism ; DNA Damage/drug effects ; DNA Damage/physiology ; DNA Repair/drug effects ; DNA Repair/physiology ; HeLa Cells ; Humans ; Methylnitronitrosoguanidine/pharmacology ; MutL Protein Homolog 1 ; MutS Homolog 2 Protein/genetics ; MutS Homolog 2 Protein/metabolism ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Proliferating Cell Nuclear Antigen/genetics ; Proliferating Cell Nuclear Antigen/metabolism ; Proteasome Endopeptidase Complex/genetics ; Proteasome Endopeptidase Complex/metabolism ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination/drug effects ; Ubiquitination/physiology
Chemical Substances	Adaptor Proteins, Signal Transducing ; CDKN1A protein, human ; Chromatin ; Cyclin-Dependent Kinase Inhibitor p21 ; DTL protein, human ; MLH1 protein, human ; Nuclear Proteins ; Proliferating Cell Nuclear Antigen ; Methylnitronitrosoguanidine (12H3O2UGSF) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; MSH2 protein, human (EC 3.6.1.3) ; MutL Protein Homolog 1 (EC 3.6.1.3) ; MutS Homolog 2 Protein (EC 3.6.1.3)
Language	English
Publishing date	2011-07-02
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M111.221341
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Article ; Online: Failure of cell cleavage induces senescence in tetraploid primary cells.

Panopoulos, Andreas / Pacios-Bras, Cristina / Choi, Justin / Yenjerla, Mythili / Sussman, Mark A / Fotedar, Rati / Margolis, Robert L

Molecular biology of the cell

2014 Volume 25, Issue 20, Page(s) 3105–3118

Abstract: Tetraploidy can arise from various mitotic or cleavage defects in mammalian cells, and inheritance of multiple centrosomes induces aneuploidy when tetraploid cells continue to cycle. Arrest of the tetraploid cell cycle is therefore potentially a critical ...

Abstract	Tetraploidy can arise from various mitotic or cleavage defects in mammalian cells, and inheritance of multiple centrosomes induces aneuploidy when tetraploid cells continue to cycle. Arrest of the tetraploid cell cycle is therefore potentially a critical cellular control. We report here that primary rat embryo fibroblasts (REF52) and human foreskin fibroblasts become senescent in tetraploid G1 after drug- or small interfering RNA (siRNA)-induced failure of cell cleavage. In contrast, T-antigen-transformed REF52 and p53+/+ HCT116 tumor cells rapidly become aneuploid by continuing to cycle after cleavage failure. Tetraploid primary cells quickly become quiescent, as determined by loss of the Ki-67 proliferation marker and of the fluorescent ubiquitination-based cell cycle indicator/late cell cycle marker geminin. Arrest is not due to DNA damage, as the γ-H2AX DNA damage marker remains at control levels after tetraploidy induction. Arrested tetraploid cells finally become senescent, as determined by SA-β-galactosidase activity. Tetraploid arrest is dependent on p16INK4a expression, as siRNA suppression of p16INK4a bypasses tetraploid arrest, permitting primary cells to become aneuploid. We conclude that tetraploid primary cells can become senescent without DNA damage and that induction of senescence is critical to tetraploidy arrest.
MeSH term(s)	Animals ; Cell Cycle/physiology ; Cells, Cultured ; Cellular Senescence/physiology ; Cyclin-Dependent Kinase Inhibitor p16/metabolism ; Fibroblasts/metabolism ; Humans ; Mitosis ; RNA, Small Interfering/genetics ; Rats ; Tetraploidy ; Tumor Suppressor Protein p53/metabolism
Chemical Substances	Cyclin-Dependent Kinase Inhibitor p16 ; RNA, Small Interfering ; Tumor Suppressor Protein p53
Language	English
Publishing date	2014-08-20
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E14-03-0844
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Article ; Online: Autophagy is required for G₁/G₀ quiescence in response to nitrogen starvation in Saccharomyces cerevisiae.

An, Zhenyi / Tassa, Amina / Thomas, Collin / Zhong, Rui / Xiao, Guanghua / Fotedar, Rati / Tu, Benjamin P / Klionsky, Daniel J / Levine, Beth

Autophagy

2014 Volume 10, Issue 10, Page(s) 1702–1711

Abstract: In response to starvation, cells undergo increased levels of autophagy and cell cycle arrest but the role of autophagy in starvation-induced cell cycle arrest is not fully understood. Here we show that autophagy genes regulate cell cycle arrest in the ... ...

Abstract	In response to starvation, cells undergo increased levels of autophagy and cell cycle arrest but the role of autophagy in starvation-induced cell cycle arrest is not fully understood. Here we show that autophagy genes regulate cell cycle arrest in the budding yeast Saccharomyces cerevisiae during nitrogen starvation. While exponentially growing wild-type yeasts preferentially arrest in G₁/G₀ in response to starvation, yeasts carrying null mutations in autophagy genes show a significantly higher percentage of cells in G₂/M. In these autophagy-deficient yeast strains, starvation elicits physiological properties associated with quiescence, such as Snf1 activation, glycogen and trehalose accumulation as well as heat-shock resistance. However, while nutrient-starved wild-type yeasts finish the G₂/M transition and arrest in G₁/G 0₀ autophagy-deficient yeasts arrest in telophase. Our results suggest that autophagy is crucial for mitotic exit during starvation and appropriate entry into a G₁/G₀ quiescent state.
MeSH term(s)	Autophagy/drug effects ; G1 Phase/drug effects ; Nitrogen/deficiency ; Nitrogen/pharmacology ; Phenotype ; Resting Phase, Cell Cycle/drug effects ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/drug effects ; Saccharomyces cerevisiae/growth & development
Chemical Substances	Nitrogen (N762921K75)
Language	English
Publishing date	2014-08-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.4161/auto.32122
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Article: Role of p21WAF1 in the cellular response to UV.

Fotedar, Rati / Bendjennat, Mourad / Fotedar, Arun

Cell cycle (Georgetown, Tex.)

2004 Volume 3, Issue 2, Page(s) 134–137

Abstract: UV or g irradiation mediated DNA damage activates p53 and induces cell cycle arrest. Induction of cyclin dependent kinase inhibitor p21WAF1 by p53 after DNA damage plays an important role in cell cycle arrest after gamma irradiation. The p53 mediated ... ...

Abstract	UV or g irradiation mediated DNA damage activates p53 and induces cell cycle arrest. Induction of cyclin dependent kinase inhibitor p21WAF1 by p53 after DNA damage plays an important role in cell cycle arrest after gamma irradiation. The p53 mediated cell cycle arrest has been postulated to allow cells to repair the DNA damage. Repair of UV damaged DNA occurs primarily by the nucleotide excision pathway (NER). It is known that p21WAF1 binds PCNA and inhibits PCNA function in DNA replication. PCNA is also required for repair by NER but there have been conflicting reports on whether p21WAF1 can inhibit PCNA function in NER. It has therefore been difficult to integrate the UV induced cell cycle arrest by p21 in the context of repair of UV damaged DNA. A recent study reported that p21WAF1 protein is degraded after low but not high doses of UV irradiation, that cell cycle arrest after UV is p21 independent, and that at low dose UV irradiation p21WAF1 degradation is essential for optimal DNA repair. These findings shed new light on the role of p21 in the cellular response to UV and clarify some outstanding issues concerning p21WAF1 function.
MeSH term(s)	Animals ; Cell Cycle/physiology ; Cell Cycle/radiation effects ; Checkpoint Kinase 1 ; Cyclin-Dependent Kinase Inhibitor p21 ; Cyclins/metabolism ; DNA Damage/physiology ; DNA Damage/radiation effects ; DNA Repair/physiology ; Humans ; Proliferating Cell Nuclear Antigen/metabolism ; Protein Kinases/metabolism ; Tumor Suppressor Protein p53/metabolism ; Tumor Suppressor Protein p53/radiation effects ; Ubiquitin/metabolism ; Ultraviolet Rays ; cdc25 Phosphatases/metabolism
Chemical Substances	CDKN1A protein, human ; Cyclin-Dependent Kinase Inhibitor p21 ; Cyclins ; Proliferating Cell Nuclear Antigen ; Tumor Suppressor Protein p53 ; Ubiquitin ; Protein Kinases (EC 2.7.-) ; Checkpoint Kinase 1 (EC 2.7.11.1) ; CDC25A protein, human (EC 3.1.3.48) ; cdc25 Phosphatases (EC 3.1.3.48)
Language	English
Publishing date	2004-01-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	2146183-1
ISSN	1551-4005 ; 1538-4101 ; 1554-8627
ISSN (online)	1551-4005
ISSN	1538-4101 ; 1554-8627
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