Literature DB >> 32561134

The multiple functions of the co-chaperone stress inducible protein 1.

Anna Carolina Carvalho da Fonseca1, Diana Matias2, Luiz Henrique Medeiros Geraldo3, Felipe Saceanu Leser4, Iohana Pagnoncelli4, Celina Garcia4, Rackele Ferreira do Amaral4, Barbara Gomes da Rosa4, Izabella Grimaldi4, Eduardo Sabino de Camargo Magalhães5, Valentín Cóppola-Segovia6, Evellyn Mayla de Azevedo6, Silvio Marques Zanata6, Flavia Regina Souza Lima7.   

Abstract

Stress inducible protein 1 (STI1) is a co-chaperone acting with Hsp70 and Hsp90 for the correct client proteins' folding and therefore for the maintenance of cellular homeostasis. Besides being expressed in the cytosol, STI1 can also be found both in the cell membrane and the extracellular medium playing several relevant roles in the central nervous system (CNS) and tumor microenvironment. During CNS development, in association with cellular prion protein (PrPc), STI1 regulates crucial events such as neuroprotection, neuritogenesis, astrocyte differentiation and survival. In cancer, STI1 is involved with tumor growth and invasion, is undoubtedly a pro-tumor factor, being considered as a biomarker and possibly therapeutic target for several malignancies. In this review, we discuss current knowledge and new findings on STI1 function as well as its role in tissue homeostasis, CNS and tumor progression.
Copyright © 2020 Elsevier Ltd. All rights reserved.

Entities:  

Keywords:  Cancer; Co-chaperone; Glia; Neuron; STI1; STIP1

Year:  2020        PMID: 32561134     DOI: 10.1016/j.cytogfr.2020.06.003

Source DB:  PubMed          Journal:  Cytokine Growth Factor Rev        ISSN: 1359-6101            Impact factor:   7.638


  3 in total

1.  The STI1-domain is a flexible alpha-helical fold with a hydrophobic groove.

Authors:  Michelle Y Fry; Shyam M Saladi; William M Clemons
Journal:  Protein Sci       Date:  2021-03-04       Impact factor: 6.725

Review 2.  The Hsp70-Hsp90 go-between Hop/Stip1/Sti1 is a proteostatic switch and may be a drug target in cancer and neurodegeneration.

Authors:  Kaushik Bhattacharya; Didier Picard
Journal:  Cell Mol Life Sci       Date:  2021-10-22       Impact factor: 9.261

3.  Altered cellular localisation and expression, together with unconventional protein trafficking, of prion protein, PrPC, in type 1 diabetes.

Authors:  Helmut Hiller; Changjun Yang; Dawn E Beachy; Irina Kusmartseva; Eduardo Candelario-Jalil; Amanda L Posgai; Harry S Nick; Desmond Schatz; Mark A Atkinson; Clive H Wasserfall
Journal:  Diabetologia       Date:  2021-07-17       Impact factor: 10.122

  3 in total

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