The nuclear matrix shell proteome of human epidermis

Warters, Raymond L.; Cassidy, Pamela B.; Sunseri, Jeremy A.; Parsawar, Krishna; Zhuplatov, Sergey; Kramer, Gwen; Leachman, Sancy A.

doi:10.1016/j.jdermsci.2010.03.001

Cited by 3 publications

(2 citation statements)

References 39 publications

(52 reference statements)

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“…lamin A/C and B, Numa, matrin-3) and many proteins involved in RNA metabolism. These observations are entirely consistent with results from a number of recent proteomic studies that characterize nuclear matrix proteins from embryonic stem cells, tumor cell types and plant cells (Oehr, 2003;Calikowski et al, 2003;Barboro et al, 2009;Albrethsen et al, 2010;Nasrabadi et al, 2010;Warters et al, 2010).…”

Section: Discussionsupporting

confidence: 89%

Subnuclear domain proteins in cancer cells support transcription factor RUNX2 functions in DNA damage response

Yang

Quaresma

Nickerson

et al. 2015

Journal of Cell Science

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Cancer cells exhibit modifications in nuclear architecture and transcriptional control. Tumor growth and metastasis are supported by RUNX family transcriptional scaffolding proteins, which mediate the assembly of nuclear-matrix-associated generegulatory hubs. We used proteomic analysis to identify RUNX2-dependent protein-protein interactions associated with the nuclear matrix in bone, breast and prostate tumor cell types and found that RUNX2 interacts with three distinct proteins that respond to DNA damage -RUVBL2, INTS3 and BAZ1B. Subnuclear foci containing these proteins change in intensity or number following UV irradiation. Furthermore, RUNX2, INTS3 and BAZ1B form UVresponsive complexes with the serine-139-phosphorylated isoform of H2AX (cH2AX). UV irradiation increases the interaction of BAZ1B with cH2AX and decreases histone H3 lysine 9 acetylation levels, which mark accessible chromatin. RUNX2 depletion prevents the BAZ1B-cH2AX interaction and attenuates loss of H3K9 and H3K56 acetylation. Our data are consistent with a model in which RUNX2 forms functional complexes with BAZ1B, RUVBL2 and INTS3 to mount an integrated response to DNA damage. This proposed cytoprotective function for RUNX2 in cancer cells might clarify its expression in chemotherapy-resistant and/or metastatic tumors.

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Section: Discussionsupporting

confidence: 89%

Subnuclear domain proteins in cancer cells support transcription factor RUNX2 functions in DNA damage response

Yang

Quaresma

Nickerson

et al. 2015

Journal of Cell Science

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“…Protein bands that were visible in the lanes with the LOX-1 affinity isolation products were excised, destained as per the manufacturer’s protocol, and sent to the University of Utah Mass Spectrometry and Proteomics core facility for analysis by liquid chromatography combined with tandem mass spectrometry (LC/MS/MS). In-gel digestion and LC/MS/MS analysis of these samples were performed as previously described [31]. …”

Section: Methodsmentioning

confidence: 99%

Chaperonin‐containing TCP‐1 complex directly binds to the cytoplasmic domain of the LOX‐1 receptor

Bakthavatsalam¹,

Soung

Tweardy

et al. 2014

FEBS Letters

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Lectin-like oxidized low-density lipoprotein receptor (LOX-1) is a scavenger receptor that binds oxidized low-density lipoprotein (OxLDL) and has a role in atherosclerosis development. The N-terminus intracellular region (cytoplasmic domain) of LOX-1 mediates receptor internalization and trafficking, potentially through intracellular protein interactions. Using affinity isolation, we identified 6 of the 8 components of the chaperonin-containing TCP-1 (CCT) complex bound to LOX-1 cytoplasmic domain, which we verified by coimmunoprecipitation and immunostaining in human umbilical vein endothelial cells. We found that the interaction between CCT and LOX-1 is direct and ATP-dependent and that OxLDL suppressed this interaction. Understanding the association between LOX-1 and the CCT complex may facilitate the design of novel therapies for cardiovascular disease.

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Myelin proteomics: the past, the unexpected and the future

Panfoli

Bruschi

Santucci

et al. 2014

Expert Review of Proteomics

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Myelin proteomics has been the subject of intense research over the last decade, and its profiling has achieved good results by both in-gel and mass spectrometry-based techniques. 1280 proteins have been identified, a number expected to increase. Some of the identified proteins are as yet not established as true components of myelin. There appears to be a limit in our ability to discover markers of myelin biogenesis, function and disease. Myelin can be easily isolated free of contaminants, thanks to its lipidic nature, which however necessitates pretreatment with detergents before mass spectrometry analysis. Here, the key issue of solubilization of myelin proteins for mass spectrometry measurements is addressed. An in-depth characterization of the myelin proteome would have a profound impact on our knowledge of its pathology and physiology. Future quantitative proteomic studies of the low-abundance myelin protein complement, likely representing key regulatory components, may in future provide molecular description of the dysmyelinating/demyelinating diseases.

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The nuclear matrix shell proteome of human epidermis

Cited by 3 publications

References 39 publications

Subnuclear domain proteins in cancer cells support transcription factor RUNX2 functions in DNA damage response

Subnuclear domain proteins in cancer cells support transcription factor RUNX2 functions in DNA damage response

Chaperonin‐containing TCP‐1 complex directly binds to the cytoplasmic domain of the LOX‐1 receptor

Myelin proteomics: the past, the unexpected and the future

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