Cited by 182Heat shock proteins researchCell death mechanisms and regulationMitochondrial Function and Pathology

Extramitochondrial localization of mortalin/mthsp70/PBP74/GRP75

Ran, Qitao, Wadhwa, Renu, Kawai, Rena, Kaul, Sunil C., Sifers, Richard N., Bick, Roger J., Smith, James R., Pereira-Smith, Olivia M.·2000·Biochemical and Biophysical Research Communications

Abstract

Subcellular fractionation and immunofluorescence microscopy were used to identify the specific sites of intracellular residence of mortalin, also called a mitochondrial homologue of the hsp70 family, in immortal human cell lines previously assigned to four distinct complementation groups (A-D) for indefinite cell division. In addition to the mitochondria it was seen in the endoplasmic reticulum (ER) fractions of all the cell lines analyzed. Interestingly, three of the group A cells lines (EJ, GM639, and HT1080), in addition to the mitochondria and ER, exhibited cytosolically (extra-organelle) localized pool of mortalin. These findings demonstrate that mortalin is not present exclusively in mitochondria. Its residence in different organelles may be the basis of differential distribution observed previously in different human cell lines.

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Crossref · 10.1006/bbrc.2000.3237

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  • The hsp70 protein family and the HSPA9 gene play a role as a downstream mediator of erythropoietin signaling and contribute to normal erythropoiesis.

    “Moreover, the hsp70 protein family and the heat shock 70kDa protein 9 (HSPA9) gene play a role as a downstream mediator of erythropoietin signaling and contribute to normal erythropoiesis (Singh et al., 1997; Ran et al., 2000; Ohtsuka et al., 2007; Chen et al., 2011).”

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References 39 · Cited by 182

Authors
Ran, Q., Wadhwa, R., Kawai, R., Kaul, S. C., Sifers, R. N., Bick, R. J., Smith, J. R., & Pereira-Smith, O. M.
Affiliations
  • Baylor College of Medicine (US)
  • Chugai Pharmaceutical Co., Ltd. (Japan) (JP)
  • The University of Texas Health Science Center at Houston (US)
Venue
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Published
2000-08
Volume
275
Issue
1
Pages
174-179
ISSN
0006-291X (ISSN-L)
OpenAlex
W2059280132
Cited by
182
References
39
Citations by year
2026: 3 · 2025: 3 · 2024: 7 · 2023: 5 · 2022: 10 · 2021: 8 · 2020: 8 · 2019: 10 · 2018: 3 · 2017: 9 · 2016: 5 · 2015: 8 · 2014: 5 · 2013: 9 · 2012: 19
FWCI
1.79
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemical and Biophysical Research Communications (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5p01ag013663-05, 5r37ag005333-18)
  • National Institute on Aging (P01-AG13663, R37-AG05333)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Keywords
mortalin, HSP70 family, GRP75, subcellular localization, mitochondria, endoplasmic reticulum, complementation groups, organelle distribution
MeSH terms
Cell Fractionation, Cell Line, Centrifugation, Density Gradient, Cytosol, Endoplasmic Reticulum, Fluorescent Antibody Technique, Humans, Mitochondria, Blotting, Western, Biomarkers, Microscopy, Immunoelectron, Microscopy, Confocal, HSP70 Heat-Shock Proteins, Mitochondrial Proteins

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