Literature DB >> 16331677

SEL1L a multifaceted protein playing a role in tumor progression.

Ida Biunno1, Monica Cattaneo, Rosaria Orlandi, Cristina Canton, Laura Biagiotti, Stefano Ferrero, Massimo Barberis, Serenella M Pupa, Aldo Scarpa, Sylvie Ménard.   

Abstract

Since the cloning in 1997 of SEL1L, the human ortholog of the sel-1 gene of C. elegans, most studies have focused on its role in cancer progression and have provided significant evidences to link its increased expression to a decrease in tumor aggressiveness. SEL1L resides on a "Genome Desert area" on chromosome 14q24.3-31 and is highly conserved in evolution. The function of the SEL1L encoded protein is still very elusive although, several evidences from lower organisms indicate that it plays a major role in protein degradation using the ubiquitin-proteosome system. SEL1L has a very complex structure made up of modules: genomically it consists of 21 exons featuring several alternative transcripts encoding for putative protein isoforms. This structural complexity ensures protein flexibility and specificity, indeed the protein was found in different sub-cellular compartments and may turn on a particular transcript in response to specific stimuli. The overall architecture of SEL1L guarantees an exquisite regulation in the expression of the gene. Copyright 2005 Wiley-Liss, Inc.

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Year:  2006        PMID: 16331677     DOI: 10.1002/jcp.20574

Source DB:  PubMed          Journal:  J Cell Physiol        ISSN: 0021-9541            Impact factor:   6.384


  23 in total

1.  Selective targeting of proteins within secretory pathway for endoplasmic reticulum-associated degradation.

Authors:  Lara Vecchi; Gianluca Petris; Marco Bestagno; Oscar R Burrone
Journal:  J Biol Chem       Date:  2012-04-20       Impact factor: 5.157

Review 2.  Missing link between microRNA and prostate cancer.

Authors:  Balraj Singh Gill; Jimi Marin Alex; Sanjeev Kumar
Journal:  Tumour Biol       Date:  2016-01-28

3.  Sel1L is indispensable for mammalian endoplasmic reticulum-associated degradation, endoplasmic reticulum homeostasis, and survival.

Authors:  Shengyi Sun; Guojun Shi; Xuemei Han; Adam B Francisco; Yewei Ji; Nuno Mendonça; Xiaojing Liu; Jason W Locasale; Kenneth W Simpson; Gerald E Duhamel; Sander Kersten; John R Yates; Qiaoming Long; Ling Qi
Journal:  Proc Natl Acad Sci U S A       Date:  2014-01-22       Impact factor: 11.205

4.  SEL1L protein critically determines the stability of the HRD1-SEL1L endoplasmic reticulum-associated degradation (ERAD) complex to optimize the degradation kinetics of ERAD substrates.

Authors:  Yasutaka Iida; Tsutomu Fujimori; Katsuya Okawa; Kazuhiro Nagata; Ikuo Wada; Nobuko Hosokawa
Journal:  J Biol Chem       Date:  2011-03-24       Impact factor: 5.157

5.  Crystallization and preliminary X-ray diffraction analysis of the Sel1-like repeats of SEL1L.

Authors:  Hanbin Jeong; Hakbong Lee; Changwook Lee
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2014-11-14       Impact factor: 1.056

6.  Cell and tissue microarray technologies for protein and nucleic acid expression profiling.

Authors:  Marina Cardano; Giuseppe R Diaferia; Maurizio Falavigna; Chiara C Spinelli; Fausto Sessa; Pasquale DeBlasio; Ida Biunno
Journal:  J Histochem Cytochem       Date:  2012-11-19       Impact factor: 2.479

7.  Down-modulation of SEL1L, an unfolded protein response and endoplasmic reticulum-associated degradation protein, sensitizes glioma stem cells to the cytotoxic effect of valproic acid.

Authors:  Monica Cattaneo; Simona Baronchelli; Davide Schiffer; Marta Mellai; Valentina Caldera; Gloria Jotti Saccani; Leda Dalpra; Antonio Daga; Rosaria Orlandi; Pasquale DeBlasio; Ida Biunno
Journal:  J Biol Chem       Date:  2013-12-05       Impact factor: 5.157

8.  mSEL-1L (Suppressor/enhancer Lin12-like) protein levels influence murine neural stem cell self-renewal and lineage commitment.

Authors:  Marina Cardano; Giuseppe R Diaferia; Monica Cattaneo; Sara S Dessì; Qiaoming Long; Luciano Conti; Pasquale Deblasio; Elena Cattaneo; Ida Biunno
Journal:  J Biol Chem       Date:  2011-03-31       Impact factor: 5.157

9.  sel-11 and cdc-42, two negative modulators of LIN-12/Notch activity in C. elegans.

Authors:  Min Sung Choi; Andrew S Yoo; Iva Greenwald
Journal:  PLoS One       Date:  2010-07-29       Impact factor: 3.240

10.  Proteome analysis of Plasmodium falciparum extracellular secretory antigens at asexual blood stages reveals a cohort of proteins with possible roles in immune modulation and signaling.

Authors:  Meha Singh; Paushali Mukherjee; Krishnamoorthy Narayanasamy; Reena Arora; Som Dutta Sen; Shashank Gupta; Krishnamurthy Natarajan; Pawan Malhotra
Journal:  Mol Cell Proteomics       Date:  2009-06-03       Impact factor: 5.911

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