Cytoskeletal Association of the A and B Nucleoside Diphosphate Kinases of Interphasic But Not Mitotic Human Carcinoma Cell Lines: Specific Nuclear Localization of the B Subunit

Pinon, Véronique Phung-Ba; Millot, Guy; Munier, Annie; Vassy, Jany; Linares-Cruz, Gustavo; Capeau, Jacqueline; Calvo, Fabien; Lacombe, Marie−Lise

doi:10.1006/excr.1998.4318

Cited by 80 publications

(57 citation statements)

References 58 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…31 After washing with HBSS, the cells were permeabilized by incubating with 0.1% Triton X-100 in HBSS for 10 min at room temperature before immunostaining. Nonspecific protein absorption was inhibited by incubation of the cells for 1 h in HBSS containing 3% BSA, 0.2% Tween 20, and 0.2% gelatin.…”

Section: Immuno¯uorescence Microscopymentioning

confidence: 99%

Rac1 regulates heat shock responses by reorganization of vimentin filaments: Identification using MALDI-TOF MS

et al. 2001

View full text Add to dashboard Cite

Rac1 has been implicated in a wide variety of biological processes, including actin remodeling and various signaling cascades. Here we have examined whether Rac1 might be involved in heat shock-induced cell signaling. We found that Rat2 stable cells expressing a dominant negative Rac1 mutant, RacN17 (Rat2-RacN17), were significantly more tolerant to heat shock than control Rat2 cells, and simultaneously inhibited the activation of SAPK/JNK by heat shock compared to control Rat2 cells. However, no discernible effect was observed in typical heat shock responses including total protein synthesis and heat shock protein synthesis. To identify the proteins involved in this difference, we separated the proteins of both Rat2 and Rat2-RacN17 cell lines after heat shock using two-dimensional gel electrophoresis and identified the differentially expressed proteins by matrix assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF MS) after in-gel trypsin digestion. Differentially expressed proteins between two cell lines were identified as vimentin. Rat2-RacN17 cells showed significant changes in vimentin as well as marked changes in vimentin reorganization by heat shock. The vimentin changes were identified as N-terminal head domain cleavage. These results suggest that Rac1 plays a pivotal role in the heat shockinduced signaling cascade by modifying intermediate vimentin filaments. Cell Death and Differentiation (2001) 8, 1093 ± 1102.

show abstract

Section: Immuno¯uorescence Microscopymentioning

confidence: 99%

Rac1 regulates heat shock responses by reorganization of vimentin filaments: Identification using MALDI-TOF MS

et al. 2001

View full text Add to dashboard Cite

show abstract

“…46,47 Accumulating evidence suggests that cytosolic NME/NDPKs NME1 but also often NME2, interact with and affect different components and regulators of the cytoskeleton, including actin-binding proteins, intermediate filaments, and cytoskeleton attachment structures (adherens junctions, desmosomes, and focal adhesions) in cells from a variety of organisms and tissues, and in the course of development, suggesting that this association is evolutionarily conserved and may serve an essential function. [48][49][50][51][52][53][54][55] The interactions of NDPK with components of the cytoskeletal machinery are highly relevant, given the well-established role of the cytoskeleton in cell motility, a critical determinant of the metastasis process. NME1 has also been reported to bind proteins belonging to small and heterotrimeric G-proteins ( [56][57][58][59][60][61] ; and Filic 62 upcoming issue; Abu-Taha et al, 63 this issue), transcriptional complexes ( 64-69 ; Sharma et al, 70 Pandey and Robertson, 71 and Puts et al, 72 all in this issue), and components of signaling pathways of MAPK, [73][74][75] TGF-β [76][77][78] and Notch, 79 as well as other factors promoting invasion and metastasis ( 80,81 ; Ferrucci et al 82 upcoming issue).…”

Section: Nme In Metastasismentioning

confidence: 99%

The NDPK/NME superfamily: state of the art

Boissan

Schlattner

Lacombe

2018

Laboratory Investigation

Self Cite

View full text Add to dashboard Cite

Nucleoside diphosphate kinases (NDPK) are nucleotide metabolism enzymes encoded by NME genes (also called NM23). Given the fact that not all NME-encoded proteins are catalytically active NDPKs and that NM23 generally refers to clinical studies on metastasis, we use here NME/NDPK to denote the proteins. Since their discovery in the 1950's, NMEs/NDPKs have been shown to be involved in multiple physiological and pathological cellular processes, but the molecular mechanisms have not been fully determined. Recent progress in elucidating these underlying mechanisms has been presented by experts in the field at the 10th International Congress on the NDPK/NME/AWD protein family in October 2016 in Dubrovnik, Croatia, and is summarized in review articles or original research in this and an upcoming issue of Laboratory Investigation. Within this editorial, we discuss three major cellular processes that involve members of the multi-functional NME/NDPK family: (i) cancer and metastasis dissemination, (ii) membrane remodeling and nucleotide channeling, and iii) protein histidine phosphorylation.

show abstract

“…This would constitute the first example of such a characteristic for thioredoxins. To prove this possibility, we performed in vitro MT binding assays using 35 S-labeled in vitro translated proteins. First, translated Txl-2 and ⌬5Txl-2 proteins were analyzed for binding to brain MTs containing myelin basic proteins.…”

Section: Txl-2 a Novel Microtubule-binding Thioredoxinmentioning

confidence: 99%

“…Txl-2 and ⌬5Txl-2 bind MTs in vitro with differential affinity. A, 35 S-labeled Txl-2 and ⌬5Txl-2 were synthesized by in vitro translation and incubated with rat brain MTs. Binding reactions were pelleted through a cushion, washed, and this procedure was repeated.…”

Section: Txl-2 a Novel Microtubule-binding Thioredoxinmentioning

confidence: 99%

“…Binding of Txl-2 and ⌬5Txl-2 proteins relative to untreated samples (arbitrarily set at 100%) is indicated as percents. B, to distinguish direct from indirect MT binding, 35 S-labeled Txl-2 (lanes a-f) and ⌬5Txl-2 (lanes g-l) were synthesized by in vitro translation and incubated with purified rat brain MTs (brain MT) or with pure MTs prepared by polymerization of pure tubulin (pure MT). Pelleted MTs were washed, and supernatants and pellets were analyzed as described for A. s1, supernatant 1; s2, supernatant 2; p, pellet.…”

Section: Txl-2 a Novel Microtubule-binding Thioredoxinmentioning

confidence: 99%

See 1 more Smart Citation

Characterization of Human Thioredoxin-like 2

Sadek

Jiménez

Damdimopoulos

et al. 2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

We describe here the cloning and characterization of a novel member of the thioredoxin family, thioredoxinlike protein 2 (Txl-2). The Txl-2 open reading frame codes for a protein of 330 amino acids consisting of two distinct domains: an N-terminal domain typical of thioredoxins and a C-terminal domain belonging to the nucleoside-diphosphate kinase family, separated by a small interface domain. The Txl-2 gene spans ϳ28 kb, is organized into 11 exons, and maps at locus 3q22.3-q23. A splicing variant lacking exon 5 (⌬5Txl-2) has also been isolated. By quantitative real time PCR we demonstrate that Txl-2 mRNA is ubiquitously expressed, with testis and lung having the highest levels of expression. Unexpectedly, light and electron microscopy analyses show that the protein is associated with microtubular structures such as lung airway epithelium cilia and the manchette and axoneme of spermatids. Using in vitro translated proteins, we demonstrate that full-length Txl-2 weakly associates with microtubules. In contrast, ⌬5Txl-2 specifically binds with very high affinity brain microtubule preparations containing microtubule-binding proteins. Importantly, ⌬5Txl-2 also binds to pure microtubules, proving that it possesses intrinsic microtubule binding capability. Taken together, ⌬5Txl-2 is the first thioredoxin reported to bind microtubules and might therefore be a novel regulator of microtubule physiology.

show abstract

Cytoskeletal Association of the A and B Nucleoside Diphosphate Kinases of Interphasic But Not Mitotic Human Carcinoma Cell Lines: Specific Nuclear Localization of the B Subunit

Cited by 80 publications

References 58 publications

Rac1 regulates heat shock responses by reorganization of vimentin filaments: Identification using MALDI-TOF MS

Rac1 regulates heat shock responses by reorganization of vimentin filaments: Identification using MALDI-TOF MS

The NDPK/NME superfamily: state of the art

Characterization of Human Thioredoxin-like 2

Contact Info

Product

Resources

About