Family with sequence similarity 107: A family of stress responsive small proteins with diverse functions in cancer and the nervous system (Review)

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Abstract

Under conditions of acute stress, rapid adaptation is crucial for maximizing biological survival. The responses to environmental stress are often complex, involving numerous genes and integrating events at the cellular and organismal levels. The heat shock proteins (HSPs) are a family of highly conserved proteins that play critical roles in maintaining cell homeostasis and protecting cells under chronic and acute stress conditions. The genes for these stress-responding proteins are widely distributed in organisms, tissues and cells. HSPs participate in a variety of physiological processes and are associated with various types of disease. In this review, we focused on family with sequence similarity 107 (FAM107), a novel unique protein family that exhibits functional similarity with HSPs during the cellular stress response. This review aimed to summarize the biological properties of FAM107 in cancer and the nervous system.

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Genome Remodeling in a Basal-like Breast Cancer Metastasis and Xenograft

Li Ding, Matthew Ellis, Shunqiang Li … (2010)

Massively parallel DNA sequencing technologies provide an unprecedented ability to screen entire genomes for genetic changes associated with tumor progression. Here we describe the genomic analyses of four DNA samples from an African-American patient with basal-like breast cancer: peripheral blood, the primary tumor, a brain metastasis, and a xenograft derived from the primary tumor. The metastasis contained two de novo mutations and a large deletion not present in the primary tumor, and was significantly enriched for 20 shared mutations. The xenograft retained all primary tumor mutations, and displayed a mutation enrichment pattern that paralleled the metastasis (16 of 20 genes). Two overlapping large deletions, encompassing CTNNA1, were present in all three tumor samples. The differential mutation frequencies and structural variation patterns in metastasis and xenograft compared to the primary tumor suggest that secondary tumors may arise from a minority of cells within the primary.

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Large-scale mapping of human protein–protein interactions by mass spectrometry

Rob Ewing, PETER CHU, Fred Elisma … (2007)

Mapping protein–protein interactions is an invaluable tool for understanding protein function. Here, we report the first large-scale study of protein–protein interactions in human cells using a mass spectrometry-based approach. The study maps protein interactions for 338 bait proteins that were selected based on known or suspected disease and functional associations. Large-scale immunoprecipitation of Flag-tagged versions of these proteins followed by LC-ESI-MS/MS analysis resulted in the identification of 24 540 potential protein interactions. False positives and redundant hits were filtered out using empirical criteria and a calculated interaction confidence score, producing a data set of 6463 interactions between 2235 distinct proteins. This data set was further cross-validated using previously published and predicted human protein interactions. In-depth mining of the data set shows that it represents a valuable source of novel protein–protein interactions with relevance to human diseases. In addition, via our preliminary analysis, we report many novel protein interactions and pathway associations.

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Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel NC2-like histone fold module that interacts with the TATA-binding protein.

Yuan-Liang Wang, Francesco Faiola, Muyu Xu … (2008)

Eukaryotic GCN5 acetyltransferases influence diverse biological processes by acetylating histones and non-histone proteins and regulating chromatin and gene-specific transcription as part of multiprotein complexes. In lower eukaryotes and invertebrates, these complexes include the yeast ADA complex that is still incompletely understood; the SAGA (Spt-Ada-Gcn5 acetylase) complexes from yeast to Drosophila that are mostly coactivators; and the ATAC (Ada Two-A containing) complex, only known in Drosophila and still poorly characterized. In contrast, vertebrate organisms, express two paralogous GCN5-like acetyltransferases (GCN5 and PCAF), which have been found so far only in SAGA-type complexes referred to hereafter as the STAGA (SPT3-TAF9-GCN5/PCAF acetylase) complexes. We now report the purification and characterization of vertebrate (human) ATAC-type complexes and identify novel components of STAGA. We show that human ATAC complexes incorporate in addition to GCN5 or PCAF (GCN5/PCAF), other epigenetic coregulators (ADA2-A, ADA3, STAF36, and WDR5), cofactors of chromatin assembly/remodeling and DNA replication machineries (POLE3/CHRAC17 and POLE4), the stress- and TGFbeta-activated protein kinase (TAK1/MAP3K7) and MAP3-kinase regulator (MBIP), additional cofactors of unknown function, and a novel YEATS2-NC2beta histone fold module that interacts with the TATA-binding protein (TBP) and negatively regulates transcription when recruited to a promoter. We further identify the p38 kinase-interacting protein (p38IP/FAM48A) as a novel component of STAGA with distant similarity to yeast Spt20. These results suggest that vertebrate ATAC-type and STAGA-type complexes link specific extracellular signals to modification of chromatin structure and regulation of the basal transcription machinery.

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Journal

Journal ID (nlm-ta): Biomed Rep

Journal ID (iso-abbrev): Biomed Rep

Journal ID (publisher-id): BR

Title: Biomedical Reports

Publisher: D.A. Spandidos

ISSN (Print): 2049-9434

ISSN (Electronic): 2049-9442

Publication date (Print): May 2014

Publication date (Electronic): 27 February 2014

Publication date PMC-release: 27 February 2014

Volume: 2

Issue: 3

Pages: 321-325

Affiliations

[1 ]Department of Oncology, Ageo Central General Hospital, Ageo, Saitama 362-8588, Japan

[2 ]Center for AIDS Research, Kumamoto University, Kumamoto 860-0811, Japan

[3 ]Research Center for Child Mental Development, Kanazawa University, Kanazawa, Ishikawa 920-8640, Japan

Author notes

Correspondence to: Dr Hideo Nakajima, Department of Oncology, Ageo Central General Hospital, 1-10-10 Kashiwaza, Ageo, Saitama 362-8588, Japan, E-mail: nakajima.h@ 123456ach.or.jp . Dr Keita Koizumi, Center for Child Mental Development, Kanazawa University, 13-1 Takaramachi, Kanazawa, Ishikawa 920-8640, Japan, E-mail: kkoizumi@ 123456med.kanazawa-u.ac.jp

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Publisher ID: br-02-03-0321

DOI: 10.3892/br.2014.243

PMC ID: 3990222

PubMed ID: 24748967

SO-VID: ead0edb0-9539-4f0c-bdd8-6847acc94aed

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This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.

Family with sequence similarity 107: A family of stress responsive small proteins with diverse functions in cancer and the nervous system (Review)

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Most cited references 32

Genome Remodeling in a Basal-like Breast Cancer Metastasis and Xenograft

Large-scale mapping of human protein–protein interactions by mass spectrometry

Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel NC2-like histone fold module that interacts with the TATA-binding protein.

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