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p62 as a therapeutic target for tumor
European Journal of Medicinal Chemistry, 2020p62/SQSTM1 (hereafter as p62) is a stress-inducible cellular protein, which interacts with various signaling proteins to regulate a variety of cellular functions. Growing lines of evidence supported a critical role of p62 in tumorigenesis, and p62 may become a therapeutic target for tumor. In this review, we summarize biological functions of structural
Qidong You, Zheng-Yu Jiang
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Presenilin-1 Regulates the Expression of p62 to Govern p62-dependent Tau Degradation
Molecular Neurobiology, 2013 Mutations in presenilin-1 (PS1) are tightly associated with early-onset familial Alzheimer's disease (FAD), which is characterized by extracellular amyloid plaques and the accumulation of intracellular Tau. In addition to being the catalytic subunit of γ-secretase, PS1 has been shown to regulate diverse cellular functions independent of its proteolytic
Ying-Tsen, Tung +6 more
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Interaction Domains of p62: A Bridge Between p62 and Selective Autophagy
DNA and Cell Biology, 2013p62 is a multidomain protein that contains different kinds of protein-protein interaction domains, including an N-terminal PB1 domain, a ZZ-type zinc finger domain, a nuclear localization signal (NLS), an export motif (NES), the LC3-interacting region (LIR), the KEAP1-interacting region (KIR), and a C-terminal Ub-associated domain (UBA).
Xiaolong, Lin +6 more
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Selective degradation of p62 by autophagy
Seminars in Immunopathology, 2010The autophagy-lysosome pathway is a highly conserved bulk degradation system in eukaryotes. During starvation, cytoplasmic constituents are non-selectively degraded by autophagy, and the resulting amino acids are utilized for cell survival. By taking advantage of mouse genetics, many physiological functions of mammalian autophagy have been uncovered ...
Yoshinobu, Ichimura, Masaaki, Komatsu
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An Evaluation of Sialation of the Nucleoporin p62
Archives of Biochemistry and Biophysics, 1998Many nuclear and cytosolic proteins are modified by single residues of O-linked N-acetyl-D-glucosamine. These include many proteins found in nuclear pore complexes required for transport of macromolecules between the nucleus and the cytoplasm. The best characterized pore glycoprotein, p62, mediates its function as one component of a protein complex ...
B, Fang, J A, Hanover, M W, Miller
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p62, an autophagy hero or culprit?
Nature Cell Biology, 2010The p62 protein recognizes toxic cellular waste, which is then scavenged by a sequestration process known as self-eating or autophagy. Lack of autophagy leads to accumulation of p62, which is not good for liver cells, as it induces a cellular stress response that leads to disease.
Tor Erik, Rusten, Harald, Stenmark
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Sequestosome 1/p62: across diseases
Biomarkers, 2012Sequestosome 1/p62 is a signal modulator or adaptor protein involved in receptor-mediated signal transduction. Sequestosome 1/p62 is gaining attention as it is involved in several diseases including Parkinson disease, Alzheimer disease, liver and breast cancer, Paget's disease of bone, obesity and insulin resistance.
Thangiah, Geetha +3 more
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Detection of p62 on Paraffin Sections by Immunohistochemistry
Cold Spring Harbor Protocols, 2015The study of autophagy in human disease is a rapidly expanding field. Diagnostic paraffin sections of a variety of patient tissues, including bone marrow, are available to researchers—yet are unsuitable for traditional autophagy quantification methods such as western blot or electron microscopy.
Alexander S, Watson +1 more
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1995
Abstract The amino-terminal half of p62 contains a domain with predicted RNA binding properties (Wong etal. 1992). This domain is highly related to a domain found in the Artemia hnRNP protein GRP33. In the C-terminal domain, a region containing 12 arginine-glycine pairs was identified: this is a characteristic of other RNA binding ...
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Abstract The amino-terminal half of p62 contains a domain with predicted RNA binding properties (Wong etal. 1992). This domain is highly related to a domain found in the Artemia hnRNP protein GRP33. In the C-terminal domain, a region containing 12 arginine-glycine pairs was identified: this is a characteristic of other RNA binding ...
openaire +1 more source