Current Focused Research: The interphase nucleus is characterized by the presence of nuclear matrix which provides basic shape and structural integrity to the nucleus. It mainly comprises of nucleic acids and proteins as the interacting partners and is important for various cellular processes like replication, transcription, splicing, DNA damage repair and recombination. Amongst different factors involved in compaction and tethering of chromatin to nuclear proteins, Scaffold/Matrix binding proteins (MARBPs) play a central role. SMAR1 (Scaffold/Matrix attachment region 1) is one such nuclear matrix-binding protein identified from double positive mouse thymocytes (Chattopadhyay et al. 2000 Genomics). SMAR1 is a known chromatin modifier which recruits HDAC1/mSin3a repressor complex to cyclin D1 promoter and thereby inhibiting its transcription (Rampalli et al. 2005 Mol Cell Biol). Interestingly, SMAR1 is also reported to interact with p53 and play a decisive role between cell cycle arrest and and apoptosis (Sinha et al, 2010 EMBO). SMAR1 is also known to be a stress response protein, wherein it regulates the acetylation status of Ku70 by interacting with HDAC6 (Chaudhary et al. 2014 Cell Death and Disease). Additionally, SMAR1 was reported to negatively regulate alternative splicing by modulating the acetylation status of Sam68 by recruiting HDAC6 (Nakka et al. 2015 PNAS). ChIP-seq analysis suggested that SMAR1 binds and regulate miR-371-373 which is an important miRNA cluster involved in cancer and metastasis (Mathai et. al. 2016 Scientific Reports). We have also reported that SMAR1 governs the switch between effector T cells and regulatory T cells by allowing the commitment of T cells to Th2 lineage and suppressing the Th1 and Th17 lineage commitment. (Mirlekar et.al. 2015 Mucosal Immunology, Mirlekar et. al. 2017 Frontiers in Immunology). It has also been observed that with the progression in grades of breast carcinoma, there is a drastic reduction in levels of SMAR1 (Singh et al, 2007 PLoS One). Recently we reported that in higher grades of colorectal cancers, reactivation of Wnt/β-Catenin results in proteasomal degradation of SMAR1 through D boxes (Taye et. al. 2018 Oncotarget). The proteosomal machinery that is involved in degradation of SMAR1 involves CDC20, which is an E3 Ubiquitin Ligase that mediates this degradation. (Paul et. al. 2017 Cell Death and Disease). Amongst many different functions of SMAR1, one such study involving the role of SMAR1 in repression of hTERT will be discussed in brief.