scholarly journals Localization of p0071-interacting proteins, plakophilin-related armadillo-repeat protein-interacting protein (PAPIN) and ERBIN, in epithelial cells

Oncogene ◽  
2002 ◽  
Vol 21 (46) ◽  
pp. 7042-7049 ◽  
Author(s):  
Hideki Ohno ◽  
Susumu Hirabayashi ◽  
Toshihiko Iizuka ◽  
Hirohide Ohnishi ◽  
Toshiro Fujita ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Interacting Proteins ◽  
Interacting Protein ◽  
Repeat Protein ◽  
Armadillo Repeat

scholarly journals SGTA associates with intracellular aggregates in neurodegenerative diseases.

2020 ◽  
Author(s):  
Shun Kubota ◽  
Hiroshi Doi ◽  
Shigeru Koyano ◽  
Kenichi Tanaka ◽  
Shingo Ikeda ◽  
...  
Keyword(s):  
Neurodegenerative Diseases ◽  
Molecular Mechanisms ◽  
In Vitro Study ◽  
Interacting Proteins ◽  
Interacting Protein ◽  
Cytoplasmic Inclusions ◽  
Specific Proteins ◽  
Intracellular Aggregates ◽  
Polyq Diseases

Abstract Intracellular aggregates are a common pathological hallmark of neurodegenerative diseases such as polyglutamine (polyQ) diseases, amyotrophic lateral sclerosis (ALS), Parkinson’s disease (PD), and multiple system atrophy (MSA). Aggregates are mainly formed by aberrant disease-specific proteins and are accompanied by accumulation of other aggregate-interacting proteins. Although aggregate-interacting proteins have been considered to modulate the formation of aggregates and to be involved in molecular mechanisms of disease progression, the components of aggregate-interacting proteins remain unknown. In this study, we showed that small glutamine-rich tetratricopeptide repeat-containing protein alfa (SGTA) is an aggregate-interacting protein in neurodegenerative diseases. Immunohistochemistry showed that SGTA interacted with intracellular aggregates in Huntington disease (HD) cell models and neurons of HD model mice. We also revealed that SGTA colocalized with intracellular aggregates in postmortem brains of patients with polyQ diseases including spinocerebellar ataxia (SCA)1, SCA2, SCA3, and dentatorubral–pallidoluysian atrophy. In addition, SGTA colocalized with glial cytoplasmic inclusions in the brains of MSA patients, whereas no accumulation of SGTA was observed in neurons of PD and ALS patients. In vitro study showed that SGTA bound to polyQ aggregates through its C-terminal domain and SGTA overexpression reduced intracellular aggregates. These results suggest that SGTA may play a role in the formation of aggregates and may act as potential modifier of molecular pathological mechanisms of polyQ diseases and MSA.

Identification of an alpha-tubulin mutant of fission yeast from gamma-tubulin-interacting protein screening: genetic evidence for alpha-/gamma-tubulin interaction

2000 ◽  
Vol 113 (24) ◽  
pp. 4557-4562 ◽  
Author(s):  
A. Takeoka ◽  
M. Shimizu ◽  
T. Horio
Keyword(s):  
Fission Yeast ◽  
Central Element ◽  
Direct Interaction ◽  
Interacting Proteins ◽  
Microtubule Nucleation ◽  
Mutation Site ◽  
Interacting Protein ◽  
Alpha Tubulin ◽  
Genes Encoding ◽  
Gamma Tubulin

gamma-Tubulin has been determined to be a central element of microtubule nucleation and, thus, indispensable for cellular organization of the microtubule. Utilizing the fact that human gamma-tubulin can function in the fission yeast Schizosaccharomyces pombe, we have generated a unique mutant screening procedure which can specifically select mutants of genes encoding gamma-tubulin-interacting proteins. One of the isolated mutants, cs76, turned out to carry a mutation in the alpha 1-tubulin gene (nda2(+)). This result suggests a direct interaction between the alpha- and gamma-tubulins. We located the mutation site in the nda2 gene and characterized the mutant phenotype. Our results demonstrate the importance of the alpha-/gamma-tubulin interaction in microtubule nucleation and should complement previous knowledge.

scholarly journals δ-Catenin/NPRAP (neural plakophilin-related armadillo repeat protein) interacts with and activates sphingosine kinase 1

2004 ◽  
Vol 382 (2) ◽  
pp. 717-723 ◽  
Author(s):  
Toshitada FUJITA ◽  
Taro OKADA ◽  
Shun HAYASHI ◽  
Saleem JAHANGEER ◽  
Noriko MIWA ◽  
...  
Keyword(s):  
Cell Motility ◽  
Hippocampal Neurons ◽  
Mdck Cells ◽  
Specific Inhibitor ◽  
Sphingosine Kinase ◽  
Dependent Manner ◽  
Repeat Protein ◽  
Sphingosine 1 Phosphate ◽  
Key Enzyme ◽  
Armadillo Repeat

Sphingosine kinase (SPHK) is a key enzyme catalysing the formation of sphingosine 1-phosphate (SPP), a lipid messenger that is implicated in the regulation of a wide variety of important cellular events acting through intracellular, as well as extracellular, mechanisms. However, the molecular mechanism of intracellular actions of SPP remains unclear. Here, we have identified δ-catenin/NPRAP (neural plakophilin-related armadillo repeat protein) as a potential binding partner for SPHK1 by yeast two-hybrid screening. From co-immunoprecipitation analyses, the C-terminal portion of δ-catenin/NPRAP containing the seventh to tenth armadillo repeats was found to be required for interaction with SPHK1. Endogenous δ-catenin/NPRAP was co-localized with endogenous SPHK1 and transfected δ-catenin/NPRAP was co-localized with transfected SPHK1 in dissociated rat hippocampal neurons. MDCK (Madin–Darby canine kidney) cells stably expressing δ-catenin/NPRAP contained elevated levels of intracellular SPP. In a purified system δ-catenin/NPRAP stimulated SPHK1 in a dose-dependent manner. Furthermore, δ-catenin/NPRAP-induced increased cell motility in MDCK cells was completely inhibited by dimethylsphingosine, a specific inhibitor of SPHK1. These results strongly suggest that at least some of δ-catenin/NPRAP functions, including increased cell motility, are mediated by an SPHK–SPP signalling pathway.

scholarly journals Mechanical stretch decreases FAK phosphorylation and reduces cell migration through loss of JIP3-induced JNK phosphorylation in airway epithelial cells

2009 ◽  
Vol 297 (3) ◽  
pp. L520-L529 ◽  
Author(s):  
Leena P. Desai ◽  
Steven R. White ◽  
Christopher M. Waters
Keyword(s):  
Cell Migration ◽  
Epithelial Cells ◽  
Mechanical Strain ◽  
Mechanical Stretch ◽  
Inhibitory Effect ◽  
Airway Epithelial Cells ◽  
Airway Epithelial ◽  
Interacting Protein ◽  
Kinase Activation ◽  
Mapk Cascades

JNK is a nonreceptor kinase involved in the early events that signal cell migration after injury. However, the linkage to early signals required to initiate the migration response to JNK has not been defined in airway epithelial cells, which exist in an environment subjected to cyclic mechanical strain (MS). The present studies demonstrate that the JNK/stress-activated protein kinase-associated protein 1 (JSAP1; also termed JNK-interacting protein 3, JIP3), a scaffold factor for MAPK cascades that links JNK activation to focal adhesion kinase (FAK), are both associated and activated following mechanical injury in 16HBE14o− human airway epithelial cells and that both FAK and JIP3 phosphorylation seen after injury are decreased in cells subjected to cyclic MS. Overexpression of either wild-type (WT)-FAK or WT-JIP3 enhanced phosphorylation and kinase activation of JNK and reduced the inhibitory effect of cyclic MS. These results suggest that cyclic MS impairs signaling of cell migration after injury via a pathway that involves FAK-JIP3-JNK.

Identification of a novel ZmSBEIIb-interacting protein involved in apparent amylose synthesis

2020 ◽  
Vol 100 (6) ◽  
pp. 674-682
Author(s):  
Chao Chen ◽  
Cong Li ◽  
Wenjie Xie ◽  
Jingting Zhang ◽  
Wansi Chen ◽  
...  
Keyword(s):  
Amylose Content ◽  
Kernel Weight ◽  
Physical Interaction ◽  
Interacting Proteins ◽  
Branching Enzyme ◽  
Interacting Protein ◽  
Protein Protein Interaction ◽  
Successful Isolation ◽  
Apparent Amylose Content ◽  
Transformed Tobacco

Inhibition of the maize starch branching enzyme IIb (ZmSBEIIb) significantly alters the amylose content and grain yield in maize. Only a few ZmSBEIIb-interacting proteins involved in the starch branching process have been identified, and the understanding of this mechanism is limited. We report here the successful isolation of an Anoctamin protein, ZmSIP, that binds directly to ZmSBEIIb. In our study, the detection of interaction between ZmSIP and different truncated ZmSBEIIb baits in yeast showed that the full-length ZmSBEIIb is essential for binding. The direct protein–protein interaction could also be found in co-transformed tobacco protoplasts. Moreover, knocking out the ZmSIP gene using the CRISPR/Cas9 system could effectively increase the apparent amylose content but maintain the maize kernel weight. Thus, our results suggest that ZmSIP may be involved in the ZmSBEIIb-mediated amylose synthesis pathway through its physical interaction with ZmSBEIIb.

scholarly journals Sipl1 and Rbck1 Are Novel Eya1-Binding Proteins with a Role in Craniofacial Development

2010 ◽  
Vol 30 (24) ◽  
pp. 5764-5775 ◽  
Author(s):  
Kathrin Landgraf ◽  
Frank Bollig ◽  
Mark-Oliver Trowe ◽  
Birgit Besenbeck ◽  
Christina Ebert ◽  
...  
Keyword(s):  
Branchial Arch ◽  
Craniofacial Development ◽  
Interacting Proteins ◽  
Rt Pcr ◽  
Interacting Protein ◽  
Eyes Absent ◽  
Mechanistic Insight ◽  
Interaction Partners ◽  
Related Proteins

ABSTRACT The eyes absent 1 protein (Eya1) plays an essential role in the development of various organs in both invertebrates and vertebrates. Mutations in the human EYA1 gene are linked to BOR (branchio-oto-renal) syndrome, characterized by kidney defects, hearing loss, and branchial arch anomalies. For a better understanding of Eya1's function, we have set out to identify new Eya1-interacting proteins. Here we report the identification of the related proteins Sipl1 (Shank-interacting protein-like 1) and Rbck1 (RBCC protein interacting with PKC1) as novel interaction partners of Eya1. We confirmed the interactions by glutathione S-transferase (GST) pulldown analysis and coimmunoprecipitation. A first mechanistic insight is provided by the demonstration that Sipl1 and Rbck1 enhance the function of Eya proteins to act as coactivators for the Six transcription factors. Using reverse transcriptase PCR (RT-PCR) and in situ hybridization, we show that Sipl1 and Rbck1 are coexpressed with Eya1 in several organs during embryogenesis of both the mouse and zebrafish. By morpholino-mediated knockdown, we demonstrate that the Sipl1 and Rbck1 orthologs are involved in different aspects of zebrafish development. In particular, knockdown of one Sipl1 ortholog as well as one Rbck1 ortholog led to a BOR syndrome-like phenotype, with characteristic defects in ear and branchial arch formation.

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