Differential Complex Formation via Paralogs in the Human Sin3 Protein Interaction Network

Adams, Mark K.; Banks, Charles A.S.; Thornton, Janet; Kempf, Cassandra G.; Zhang, Ying; Miah, Sayem; Hao, Yan; Sardiu, Mihaela E.; Killer, Maxime; Hattem, Gaye; Murray, Alexis; Katt, Maria L.; Florens, Laurence; Washburn, Michael P.

doi:10.1074/mcp.ra120.002078

Cited by 32 publications

(44 citation statements)

References 50 publications

(80 reference statements)

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“…The SIN3 interactome is well studied in yeast, human, and mouse 52 , 53 . Therefore, the protein–protein interactions of these eukaryotic systems can be extrapolated to ceSIN3 ortholog with computational methods 54 .…”

Section: Resultsmentioning

confidence: 99%

SIN-3 functions through multi-protein interaction to regulate apoptosis, autophagy, and longevity in Caenorhabditis elegans

Konwar

Maini

Kohli

et al. 2022

Sci Rep

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SIN3/HDAC is a multi-protein complex that acts as a regulatory unit and functions as a co-repressor/co-activator and a general transcription factor. SIN3 acts as a scaffold in the complex, binding directly to HDAC1/2 and other proteins and plays crucial roles in regulating apoptosis, differentiation, cell proliferation, development, and cell cycle. However, its exact mechanism of action remains elusive. Using the Caenorhabditis elegans (C. elegans) model, we can surpass the challenges posed by the functional redundancy of SIN3 isoforms. In this regard, we have previously demonstrated the role of SIN-3 in uncoupling autophagy and longevity in C. elegans. In order to understand the mechanism of action of SIN3 in these processes, we carried out a comparative analysis of the SIN3 protein interactome from model organisms of different phyla. We identified conserved, expanded, and contracted gene classes. The C. elegans SIN-3 interactome -revealed the presence of well-known proteins, such as DAF-16, SIR-2.1, SGK-1, and AKT-1/2, involved in autophagy, apoptosis, and longevity. Overall, our analyses propose potential mechanisms by which SIN3 participates in multiple biological processes and their conservation across species and identifies candidate genes for further experimental analysis.

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Section: Resultsmentioning

confidence: 99%

SIN-3 functions through multi-protein interaction to regulate apoptosis, autophagy, and longevity in Caenorhabditis elegans

Konwar

Maini

Kohli

et al. 2022

Sci Rep

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“…Cluster is based upon Euclidean distance. (B) Crosslink map for the BRMS1 protein, data is extracted from SIN3A XL-MS experiments from Adams et al [ 24 ]. (C) SIN3A co-immunoprecipitation of nuclear lysates followed by MALDI-TOF mass spectrometry.…”

Section: Resultsmentioning

confidence: 99%

“…(C) SIN3A co-immunoprecipitation of nuclear lysates followed by MALDI-TOF mass spectrometry. (D) Utilizing MS results from Adams et al [ 24 ] dNSAF for SIN3A and SIN3B in relation to BRMS1 and BRMS1L.…”

Section: Resultsmentioning

confidence: 99%

“…To more clearly look at the interactions of BRMS1 and BRMS1L in association with the Sin3/HDAC complexes, we utilized normalized spectral counts of previously published mass spectrometry data [ 24 ]. We found a distinct pattern difference of BRMS1 and BRMS1L binding with SIN3A and SIN3B ( Fig 2D ).…”

Section: Resultsmentioning

confidence: 99%

“…The BRMS1 primers listed in S1 Data were used to amplify a sequence coding for BRMS1 isoform 1 (NP_056214), or for mutant versions of BRMS1 as indicated in the figure legends, using a previously reported BRMS1 construct as a template [ 24 ]. A short synthetic duplex DNA oligonucleotide (described in S1 Data ) was used to clone a short fragment of the C terminus of BRMS1 (amino acids 230–246).…”

Section: Methodsmentioning

confidence: 99%

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Perturbation of BRMS1 interactome reveals pathways that impact metastasis

et al. 2021

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Breast Cancer Metastasis Suppressor 1 (BRMS1) expression is associated with longer patient survival in multiple cancer types. Understanding BRMS1 functionality will provide insights into both mechanism of action and will enhance potential therapeutic development. In this study, we confirmed that the C-terminus of BRMS1 is critical for metastasis suppression and hypothesized that critical protein interactions in this region would explain its function. Phosphorylation status at S237 regulates BRMS1 protein interactions related to a variety of biological processes, phenotypes [cell cycle (e.g., CDKN2A), DNA repair (e.g., BRCA1)], and metastasis [(e.g., TCF2 and POLE2)]. Presence of S237 also directly decreased MDA-MB-231 breast carcinoma migration in vitro and metastases in vivo. The results add significantly to our understanding of how BRMS1 interactions with Sin3/HDAC complexes regulate metastasis and expand insights into BRMS1’s molecular role, as they demonstrate BRMS1 C-terminus involvement in distinct protein-protein interactions.

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Softly but surely: A new perspective on transcriptional repression

Plessel

Gourichon

2021

BioEssays

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Differential Complex Formation via Paralogs in the Human Sin3 Protein Interaction Network

Cited by 32 publications

References 50 publications

SIN-3 functions through multi-protein interaction to regulate apoptosis, autophagy, and longevity in Caenorhabditis elegans

SIN-3 functions through multi-protein interaction to regulate apoptosis, autophagy, and longevity in Caenorhabditis elegans

Perturbation of BRMS1 interactome reveals pathways that impact metastasis

Softly but surely: A new perspective on transcriptional repression

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