Read by QxMD icon Read


Agnieszka Hareza, Magda Bakun, Bianka Świderska, Małgorzata Dudkiewicz, Alicja Koscielny, Anna Bajur, Jacek Jaworski, Michał Dadlez, Krzysztof Pawłowski
Many kinases are still 'orphans,' which means knowledge about their substrates, and often also about the processes they regulate, is lacking. Here, DIA1/C3orf58, a member of a novel predicted kinase-like family, is shown to be present in the endoplasmic reticulum and to influence trafficking via the secretory pathway. Subsequently, DIA1 is subjected to phosphoproteomics analysis to cast light on its signalling pathways. A liquid chromatography-tandem mass spectrometry proteomic approach with phosphopeptide enrichment is applied to membrane fractions of DIA1-overexpressing and control HEK293T cells, and phosphosites dependent on the presence of DIA1 are elucidated...
2018: PeerJ
Tim B Fessenden, Yvonne Beckham, Mathew Perez-Neut, Guillermina Ramirez-San Juan, Aparajita H Chourasia, Kay F Macleod, Patrick W Oakes, Margaret L Gardel
Developing tissues change shape and tumors initiate spreading through collective cell motility. Conserved mechanisms by which tissues initiate motility into their surroundings are not known. We investigated cytoskeletal regulators during collective invasion by mouse tumor organoids and epithelial Madin-Darby canine kidney (MDCK) acini undergoing branching morphogenesis in collagen. Use of the broad-spectrum formin inhibitor SMIFH2 prevented the formation of migrating cell fronts in both cell types. Focusing on the role of the formin Dia1 in branching morphogenesis, we found that its depletion in MDCK cells does not alter planar cell motility either within the acinus or in two-dimensional scattering assays...
April 2, 2018: Journal of Cell Biology
Michael Keegan Delaney, Viacheslav Malikov, Qingqing Chai, Guangyuan Zhao, Mojgan H Naghavi
Diaphanous (Dia)-related formins (DRFs) coordinate cytoskeletal remodeling by controlling actin nucleation and microtubule (MT) stabilization to facilitate processes such as cell polarization and migration; yet the full extent of their activities remains unknown. Here, we uncover two discrete roles and functions of DRFs during early human immunodeficiency virus type 1 (HIV-1) infection. Independent of their actin regulatory activities, Dia1 and Dia2 facilitated HIV-1-induced MT stabilization and the intracellular motility of virus particles...
August 15, 2017: Proceedings of the National Academy of Sciences of the United States of America
Tae-Hun Kang, Jeong-In Baek, Borum Sagong, Hong-Joon Park, Chan Ik Park, Kyu-Yup Lee, Un-Kyung Kim
Hair cells in the cochlea display highly regulated actin polymerization, which is mediated by the human diaphanous-related formin 1 gene (DIAPH1; also called DFNA1, DIA1). DFNA1, the first type of autosomal dominant nonsyndromic hearing loss (ADNSHL), is known to be associated with mutations in DIAPH1. However, no genetic study of DFNA1 in Koreans with hearing loss has yet been reported. A 51-year-old patient in a Korean family with ADNSHL was examined by pure-tone audiometry, and genetic analysis of DIAPH1 was performed...
April 4, 2017: Genes & Genetic Systems
Takehiko Ueyama, Yuzuru Ninoyu, Shin-Ya Nishio, Takushi Miyoshi, Hiroko Torii, Koji Nishimura, Kazuma Sugahara, Hideaki Sakata, Dean Thumkeo, Hirofumi Sakaguchi, Naoki Watanabe, Shin-Ichi Usami, Naoaki Saito, Shin-Ichiro Kitajiri
DIAPH1 encodes human DIA1, a formin protein that elongates unbranched actin. The c.3634+1G>T DIAPH1 mutation causes autosomal dominant nonsyndromic sensorineural hearing loss, DFNA1, characterized by progressive deafness starting in childhood. The mutation occurs near the C-terminus of the diaphanous autoregulatory domain (DAD) of DIA1, which interacts with its N-terminal diaphanous inhibitory domain (DID), and may engender constitutive activation of DIA1. However, the underlying pathogenesis that causes DFNA1 is unclear...
November 2016: EMBO Molecular Medicine
Aline Jatho, Svenja Hartmann, Naim Kittana, Felicitas Mügge, Christina M Wuertz, Malte Tiburcy, Wolfram-Hubertus Zimmermann, Dörthe M Katschinski, Susanne Lutz
INTRODUCTION: RhoA has been shown to be beneficial in cardiac disease models when overexpressed in cardiomyocytes, whereas its role in cardiac fibroblasts (CF) is still poorly understood. During cardiac remodeling CF undergo a transition towards a myofibroblast phenotype thereby showing an increased proliferation and migration rate. Both processes involve the remodeling of the cytoskeleton. Since RhoA is known to be a major regulator of the cytoskeleton, we analyzed its role in CF and its effect on myofibroblast characteristics in 2 D and 3D models...
2015: PloS One
Glenn Björklund, Hans-Christer Holmberg, Thomas Stöggl
PURPOSE: To investigate the influence of prior high intensity double poling (DP) on physiological and biomechanical responses during subsequent diagonal stride (DIA). METHODS: Eight well-trained male cross-country skiers (age 22 ± 3 yr; VO2max 69 ± 3 ml · kg(-1) · min(-1)) roller-skied on a treadmill sequentially for 3 min at 90% DIA VO2max (DIA1), 3 min at 90% DP VO2peak and 3 min at 90% DIA VO2max (DIA2). Cardio-respiratory responses were monitored continuously and gases and metabolites in blood from the a...
2015: SpringerPlus
Vladimir Purvanov, Manuel Holst, Jameel Khan, Christian Baarlink, Robert Grosse
Homotypic or entotic cell-in-cell invasion is an integrin-independent process observed in carcinoma cells exposed during conditions of low adhesion such as in exudates of malignant disease. Although active cell-in-cell invasion depends on RhoA and actin, the precise mechanism as well as the underlying actin structures and assembly factors driving the process are unknown. Furthermore, whether specific cell surface receptors trigger entotic invasion in a signal-dependent fashion has not been investigated. In this study, we identify the G-protein-coupled LPA receptor 2 (LPAR2) as a signal transducer specifically required for the actively invading cell during entosis...
2014: ELife
Siu P Ngok, Panos Z Anastasiadis
Rho GTPases are cytoskeleton-regulating proteins that mediate the formation of intercellular junctions. Their localized activation by Rho GEFs (guanine-nucleotide exchange factors) and the selective activation of downstream effectors have emerged as areas of active research in the cell adhesion field. We reported recently that the Rho-specific GEFs Syx (Synectin-binding RhoA exchange factor) and TEM4 (Tumor Endothelial Marker 4) are both essential for endothelial junction maturation and barrier function. Syx is recruited to cell contacts via its C-terminal PDZ binding motif and it's interaction with Mupp1 and the Crumbs polarity complex, while the junctional localization of TEM4 requires it's N-terminal domain and interaction with the cadherin-catenin complex...
December 1, 2013: Tissue Barriers
R M Delorme, H T Skorupska
Chloroplastic (NADP(+)) glyceraldehyde-3-phosphate dehydrogenase (E.C. catalyzes the second reaction in photosynthesis after the fixation of carbon by RuBisCO. Chloroplast-bound (NADP(+)) G3PDH was resolved in soybean by starch gel electrophoresis using L-histidine-citrate buffer (pH 5.7). Histochemical staining revealed zymogram patterns indicative of a tetramer. A survey of soybean genotypes revealed differences in zymogram patterns between the principal cytoplasmic sources of the northern and southern US germplasms...
February 1993: TAG. Theoretical and Applied Genetics. Theoretische und Angewandte Genetik
Justus C Dachsel, Siu P Ngok, Laura J Lewis-Tuffin, Antonis Kourtidis, Rory Geyer, Lauren Johnston, Ryan Feathers, Panos Z Anastasiadis
The role of RhoA in promoting directed cell migration has been complicated by studies showing that it is activated both in the front and the rear of migrating cells. We report here that the RhoA-specific guanine nucleotide exchange factor Syx is required for the polarity of actively migrating brain and breast tumor cells. This function of Syx is mediated by the selective activation of the RhoA downstream effector Dia1, the subsequent reorganization of microtubules, and the downregulation of focal adhesions and actin stress fibers...
December 2013: Molecular and Cellular Biology
Jonathan Stricker, Yvonne Beckham, Michael W Davidson, Margaret L Gardel
Myosin II motors drive changes in focal adhesion morphology and composition in a "maturation process" that is crucial for regulating adhesion dynamics and signaling guiding cell adhesion, migration and fate. The underlying mechanisms of maturation, however, have been obscured by the intermingled effects of myosin II on lamellar actin architecture, dynamics and force transmission. Here, we show that focal adhesion growth rate stays constant even when cellular tension is reduced by 75%. Focal adhesion growth halts only when myosin stresses are sufficiently low to impair actin retrograde flow...
2013: PloS One
Laura Andrés-Delgado, Olga M Antón, Miguel Angel Alonso
T-cell antigen receptor (TCR) engagement triggers the rapid reorientation of the centrosome, which is associated with the secretory machinery, toward the immunological synapse (IS) for polarized protein trafficking. Recent evidence indicates that upon TCR triggering the INF2 formin, together with the formins DIA1 and FMNL1, promotes the formation of a specialized array of stable detyrosinated MTs that breaks the symmetrical organization of the T-cell microtubule (MT) cytoskeleton. The detyrosinated MT array and TCR-induced tyrosine phosphorylation should coincide for centrosome polarization...
2013: Frontiers in Immunology
Małgorzata Dudkiewicz, Anna Lenart, Krzysztof Pawłowski
The catalogues of protein kinases, the essential effectors of cellular signaling, have been charted in Metazoan genomes for a decade now. Yet, surprisingly, using bioinformatics tools, we predicted protein kinase structure for proteins coded by five related human genes and their Metazoan homologues, the FAM69 family. Analysis of three-dimensional structure models and conservation of the classic catalytic motifs of protein kinases present in four out of five human FAM69 proteins suggests they might have retained catalytic phosphotransferase activity...
2013: PloS One
Alrun Hotz, Yorck Hellenbroich, Jürgen Sperner, Michaela Linder-Lucht, Uta Tacke, Caren Walter, Almuth Caliebe, Inga Nagel, Dawn E Saunders, Gerhard Wolff, Peter Martin, Deborah J Morris-Rosendahl
5q14.3 deletions spanning and flanking MEF2C as well as intragenic MEF2C mutations have recently been described as a cause of severe intellectual disability, epilepsy, and muscular hypotonia, with variable brain and other anomalies. With an increasing number of patients described, the clinical presentation of the patients appears to be relatively uniform, however the structural brain phenotypes described are variable. We describe two unrelated patients with overlapping de novo interstitial deletions of 4.1 and 1...
September 2013: American Journal of Medical Genetics. Part A
Siu P Ngok, Rory Geyer, Antonis Kourtidis, Peter Storz, Panos Z Anastasiadis
Syx is a Rho-specific guanine nucleotide exchange factor (GEF) that localizes at cell-cell junctions and promotes junction stability by activating RhoA and the downstream effector Diaphanous homolog 1 (Dia1). Previously, we identified several molecules, including 14-3-3 proteins, as Syx-interacting partners. In the present study, we show that 14-3-3 isoforms interact with Syx at both its N- and C-terminal regions in a phosphorylation-dependent manner. We identify the protein kinase D-mediated phosphorylation of serine 92 on Syx, and additional phosphorylation at serine 938, as critical sites for 14-3-3 association...
March 1, 2013: Journal of Biological Chemistry
Laura Andrés-Delgado, Olga M Antón, Francesca Bartolini, Ana Ruiz-Sáenz, Isabel Correas, Gregg G Gundersen, Miguel A Alonso
T cell antigen receptor-proximal signaling components, Rho-family GTPases, and formin proteins DIA1 and FMNL1 have been implicated in centrosome reorientation to the immunological synapse of T lymphocytes. However, the role of these molecules in the reorientation process is not yet defined. Here we find that a subset of microtubules became rapidly stabilized and that their α-tubulin subunit posttranslationally detyrosinated after engagement of the T cell receptor. Formation of stabilized, detyrosinated microtubules required the formin INF2, which was also found to be essential for centrosome reorientation, but it occurred independently of T cell receptor-induced massive tyrosine phosphorylation...
September 17, 2012: Journal of Cell Biology
Tabetha M Bonacci, Dianne S Hirsch, Yi Shen, Milos Dokmanovic, Wen Jin Wu
R-cadherin is a member of the classical cadherins. Though much is known about E-cadherin in adherens junction formation in epithelial cells, the role of R-cadherin in epithelial cells remains elusive. This study examines regulation of R-cadherin adherens junctions by the small GTPase Rho and its downstream effectors in MDA-MB-231 breast cancer cells, MDA-MB-231 cells stably expressing the N-terminus of c-Cbl, and MCF10A normal breast epithelial cells. We find that the small GTPase Rho regulates R-cadherin adherens junction formation via Dia1 (also known as p140mDia) and profilin-1-mediated signaling pathway...
November 2012: Cellular Signalling
Guoning Liao, Gang Liu
Messenger RNA (mRNA) localization plays an important role in various cellular functions. To date, two general mechanisms have been identified for intracellular mRNA localization. The first one was identified by Blobel and colleagues more than three decades ago, by which mRNAs encoding for membrane and secreted proteins are targeted to the endoplasmic reticulum (ER) in a signal peptide dependent manner.1 The second mechanism is for the intracellular targeting of mRNAs encoding cytosolic proteins, which is dependent on specific sequence on the mRNA called zipcode...
September 2011: Communicative & Integrative Biology
J J Arranz, Y Bayón, I Medjugorac, F Primitivo
Thirteen biochemical blood polymorphisms were analysed in a population of 149 Spanish Avileña-Negra Ibérica cattle. The study revealed variation at the following nine loci: HBB, CA, NP, CP, AMY1, ALB, GC, TF and PTF2. The following systems were monomorphic: CAT, DIA1, MDH1 and ME1. Using polyacrylamide-gel electrophoresis, a slow, migrating pair of bands was found in the GC protein system. This pattern is probably controlled by the GC(C) allele, described in only a few cases in cattle. Furthermore, starch-gel electrophoresis allowed the detection of a variant with intermediate mobility between the ALB(A) and the ALB(B) alleles at the albumin locus...
January 12, 1994: Journal of Animal Breeding and Genetics, Zeitschrift Für Tierzüchtung und Züchtungsbiologie
Fetch more papers »
Fetching more papers... Fetching...
Read by QxMD. Sign in or create an account to discover new knowledge that matter to you.
Remove bar
Read by QxMD icon Read

Search Tips

Use Boolean operators: AND/OR

diabetic AND foot
diabetes OR diabetic

Exclude a word using the 'minus' sign

Virchow -triad

Use Parentheses

water AND (cup OR glass)

Add an asterisk (*) at end of a word to include word stems

Neuro* will search for Neurology, Neuroscientist, Neurological, and so on

Use quotes to search for an exact phrase

"primary prevention of cancer"
(heart or cardiac or cardio*) AND arrest -"American Heart Association"