scholarly journals Characterization of an ankyrin repeat-containing Shank2 isoform (Shank2E) in liver epithelial cells

2004 ◽  
Vol 380 (1) ◽  
pp. 181-191 ◽  
Author(s):  
Ryan R. McWILLIAMS ◽  
Elizabeth GIDEY ◽  
Laura FOUASSIER ◽  
Scott A. WEED ◽  
R. Brian DOCTOR
Keyword(s):  
Epithelial Cells ◽  
Apical Membrane ◽  
Ankyrin Repeat ◽  
Scaffolding Proteins ◽  
Ankyrin Repeats ◽  
Density Region ◽  
Epithelial Tissues ◽  
Liver Epithelial Cells ◽  
Repeat Domain

Shank proteins are a family of multidomain scaffolding proteins best known for their role in organizing the postsynaptic density region in neurons. Unlike Shank1 and Shank3, Shank2 [also known as Pro-SAP1 (proline-rich synapse-associated protein 1), CortBP1 (cortactin binding protein 1) or Spank-3] has been described as a truncated family member without an N-terminal ankyrin repeat domain. The present study utilized bioinformatics to demonstrate the presence of exons encoding ankyrin repeats in the region preceding the previously described Shank2 gene. cDNA sequencing of mRNA from epithelial cells revealed a novel spliceoform of Shank2, termed Shank2E, that encodes a predicted 200 kDa protein with six N-terminal ankyrin repeats. Shank2 mRNA from epithelial tissues was larger than transcripts in brain. Likewise, the apparent mass of Shank2 protein was larger in epithelial tissues (230 kDa) when compared with brain (165/180 kDa). Immunofluorescence and membrane fractionation found Shank2E concentrated at the apical membrane of liver epithelial cells. In cultured cholangiocytes, co-immunoprecipitation and detergent solubility studies revealed Shank2E complexed with actin and co-distributed with actin in detergent-insoluble lipid rafts. These findings indicate epithelial cells express an ankyrin repeat-containing Shank2 isoform, termed Shank2E, that is poised to co-ordinate actin-dependent events at the apical membrane.

Characterization of liver epithelial cells transfected withmyc and/orras oncogenes

1991 ◽  
Vol 36 (5) ◽  
pp. 642-652 ◽  
Author(s):  
Stephen C. Strom ◽  
John B. Faust ◽  
Erika Cappelluti ◽  
Robert B. Harris ◽  
Narendra D. Lalwani
Keyword(s):  
Epithelial Cells ◽  
Liver Epithelial Cells

scholarly journals A Regulated Complex of the Scaffolding Proteins PDZK1 and EBP50 with Ezrin Contribute to Microvillar Organization

2010 ◽  
Vol 21 (9) ◽  
pp. 1519-1529 ◽  
Author(s):  
David P. LaLonde ◽  
Damien Garbett ◽  
Anthony Bretscher
Keyword(s):  
Epithelial Cells ◽  
Complex Formation ◽  
Ternary Complex ◽  
Apical Membrane ◽  
Pdz Domain ◽  
Scaffolding Proteins ◽  
Pdz Domains ◽  
Zona Occludens

PDZK1 and ezrin, radixin, moesin binding phosphoprotein 50 kDa (EBP50) are postsynaptic density 95/disc-large/zona occludens (PDZ)-domain–containing scaffolding proteins found in the apical microvilli of polarized epithelial cells. Binary interactions have been shown between the tail of PDZK1 and the PDZ domains of EBP50, as well as between EBP50 and the membrane–cytoskeletal linking protein ezrin. Here, we show that these molecules form a regulated ternary complex in vitro and in vivo. Complex formation is cooperative because ezrin positively influences the PDZK1/EBP50 interaction. Moreover, the interaction of PDZK1 with EBP50 is enhanced by the occupancy of EBP50's adjacent PDZ domain. The complex is further regulated by location, because PDZK1 shuttles from the nucleus in low confluence cells to microvilli in high confluence cells, and this regulates the formation of the PDZK1/EBP50/ezrin complex in vivo. Knockdown of EBP50 decreases the presence of microvilli, a phenotype that can be rescued by EBP50 re-expression or expression of a PDZK1 chimera that is directly targeted to ezrin. Thus, when appropriately located, PDZK1 can provide a function necessary for microvilli formation normally provided by EBP50. By entering into the ternary complex, PDZK1 can both enhance the scaffolding at the apical membrane as well as augment EBP50's role in microvilli formation.

scholarly journals Characterization of the composition and functioning of the Crumbs complex in C. elegans

2021 ◽  
Author(s):  
Victoria G Castiglioni ◽  
Joao J Ramalho ◽  
Jason R Kroll ◽  
Riccardo Stucchi ◽  
Hanna van Beuzekom ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Apical Membrane ◽  
Scaffolding Protein ◽  
Animal Development ◽  
C Elegans ◽  
Apical Domain ◽  
Junction Protein ◽  
Crumbs Complex

The apical domain of epithelial cells can acquire a diverse array of morphologies and functions, which is critical for the function of epithelial tissues. The Crumbs proteins are evolutionary conserved transmembrane proteins with essential roles in promoting apical domain formation in epithelial cells. The short intracellular tail of Crumbs proteins interacts with a variety of proteins, including the scaffolding protein Pals1 (protein associated with LIN7, Stardust in Drosophila). Pals1 in turn binds to a second scaffolding protein termed PATJ (Pals1-associated tight junction protein), to form the core Crumbs/ Pals1/PATJ Crumbs complex. While essential roles in epithelial organization have been shown for Crumbs proteins in Drosophila and mammalian systems, the three Caenorhabditis elegans crumbs genes are dispensable for epithelial polarization and animal development. Moreover, the presence and functioning of orthologs of Pals1 and PATJ has not been investigated. Here, we identify MAGU-2 and MPZ-1 as the C. elegans orthologs of Pals1 and PATJ, respectively. We show that MAGU-2 interacts with all three Crumbs proteins as well as MPZ-1, and localizes to the apical membrane domain in a Crumbs-dependent fashion. Similar to crumbs mutants, a magu-2 null mutant shows no developmental or epithelial polarity defects. Finally, we show that overexpression of the Crumbs proteins EAT-20 or CRB-3 in the C. elegans intestine can lead to apical membrane expansion. Our results shed light into the composition of the C. elegans Crumbs complex and indicate that the role of Crumbs proteins in promoting apical domain identity is conserved.

scholarly journals Purification and characterization of mouse fetal liver epithelial cells with highin vivorepopulation capacity

Hepatology ◽  
2005 ◽  
Vol 42 (1) ◽  
pp. 130-139 ◽  
Author(s):  
Dirk Nierhoff ◽  
Atsushi Ogawa ◽  
Michael Oertel ◽  
Yuan-Qing Chen ◽  
David A. Shafritz
Keyword(s):  
Epithelial Cells ◽  
Fetal Liver ◽  
Purification And Characterization ◽  
Liver Epithelial Cells

Determination of Ankyrin Repeats Domain (ANK) a of RNASE L Gene in Hepatitis C Patients and its effects on Viral Load

2020 ◽  
Author(s):  
Anum Liaquat Ali
Keyword(s):  
Viral Load ◽  
Hepatitis C ◽  
Pcr Amplification ◽  
Ankyrin Repeat ◽  
Hcv Infection ◽  
Rnase L ◽  
Ankyrin Repeats ◽  
Genotype 3 ◽  
Repeat Domain ◽  
Ankyrin Repeat Domain

Background: Hepatitis C virus (HCV) is one of the major global causes of death. Different types of gene are involved as Ankyrin repeat domains of RNASE L gene. It performs a significant role in antiviral response, regulated by interferon, and involved in cleavage of RNA. Therefore, aim of this study was to identify Ankyrin repeat domain expression in Hepatitis C positive patients and correlate it with viral load of Hepatitis C. Methods: In this study, a total of 80 HCV positive patient’s whole blood samples were investigated. RNA was extracted from plasma followed by Real Time PCR for quantization of HCV viral load and genotypic analyses. DNA was also extracted from these samples followed by PCR amplification of Ankyrin repeat domain of RNASE L gene. Data was analyzed using SPSS Results: All of the patients (n=80) included in study had HCV infection. Mean age of patients was 50.86 ±14.84 years. Among them, 48(63.8%) were males and 32 (36.1%) were females. Majority of patients were males and belonged to age group 58-73 years age. All HCV infected individuals 36 (45%) had HCV genotype 3 and had viral loads mean range 837404.21 ±1302. Therefore, Ankyrin repeats domain of RNASE L gene expression was high in HCV patients sample with viral load of 17.00±15.1. Conclusion: Ankyrin repeat domain expression was observed in Hepatitis C patients and its significant correlation with viral load of Hepatitis C. Ankyrin repeat domain of RNASE L gene in conjunction with therapeutic intervention are required for establishing better strategies for controlling HCV infection.

scholarly journals Biophysical characterization of the free IκBα ankyrin repeat domain in solution

2004 ◽  
Vol 13 (7) ◽  
pp. 1767-1777 ◽  
Author(s):  
Carrie Hughes Croy ◽  
Simon Bergqvist ◽  
Tom Huxford ◽  
Gourisankar Ghosh ◽  
Elizabeth A. Komives
Keyword(s):  
Ankyrin Repeat ◽  
Biophysical Characterization ◽  
Repeat Domain ◽  
Ankyrin Repeat Domain

scholarly journals Characterization of a novel gene encoding ankyrin repeat domain from Cotesia vestalis polydnavirus (CvBV)

Virology ◽  
2008 ◽  
Vol 375 (2) ◽  
pp. 374-382 ◽  
Author(s):  
Min Shi ◽  
Ya-Feng Chen ◽  
Fang Huang ◽  
Peng-Cheng Liu ◽  
Xue-Ping Zhou ◽  
...  
Keyword(s):  
Ankyrin Repeat ◽  
Gene Encoding ◽  
Cotesia Vestalis ◽  
Novel Gene ◽  
Repeat Domain ◽  
Ankyrin Repeat Domain
Sign in / Sign up

Export Citation Format

Share Document