Role of hsp70 in cancer growth and survival

Marcus P.D. Hatfield, Sándor Lovas

Research output: Contribution to journalReview articlepeer-review

18 Scopus citations


Hsp70 is a highly conserved protein that refolds misfolded proteins and has numerous housekeeping functions which regulate apoptosis and other cell activities. Hsp70 consists of a nucleotide binding domain which binds ATP and a substrate binding domain that binds misfolded proteins. The substrate binding domain contains a peptide binding pocket which is covered by a helical lid. In humans, there are three major cytosolic Hsp70 isotypes, Hsp70-8, Hsp70-1 and Hsp70-2. Leukemic and numerous other cancer cells have a greater amount of Hsp70-1 and -2, which help the cancer cells inhibit apoptosis in response to stress. This review summarizes the structure and role of Hsp70 proteins in cancer survival.

Original languageEnglish (US)
Pages (from-to)616-624
Number of pages9
JournalProtein and Peptide Letters
Issue number6
StatePublished - Jun 2012

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry


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