Heat shock 70 kDa protein 1L (HSPA1L)

Heat shock 70 kDa protein 1L (HSPA1L) is a member of the heat shock protein 70 (Hsp70) family and acts as a molecular chaperone essential for the proper folding of newly synthesized and misfolded proteins, stabilization of proteins against aggregation, and protein homeostasis[1][3]. It is constitutively and abundantly expressed in the testis but distributed at low levels in other tissues. HSPA1L operates via cycles of ATP binding and hydrolysis, allowing substrate proteins to bind and release, supporting refolding or targeting for degradation[1][3][5]. Beyond housekeeping functions, HSPA1L and related Hsp70 proteins are implicated in processes such as signal transduction, apoptosis, and immune modulation, especially by presenting antigens to cytotoxic T cells[1]. Altered expression or dysfunction of HSPA1L has been linked to cancer, various neurodegenerative diseases (notably Parkinson’s disease), inflammatory syndromes, and graft-versus-host disease[1][2][3]. Clinically, HSPA1L can act as a prognostic and diagnostic biomarker, particularly in Parkinson’s disease and glioma[2]. Structurally, HSPA1L contains a C-terminal substrate-binding domain and an N-terminal ATP-binding domain, with both domains contributing to the regulation of its chaperone cycle[1][5].

Other names

HSP70-1LHSP70-HOMHSP70Thum70theat shock protein family A (Hsp70) member 1 likeheat shock 70 kDa protein 1-likeheat shock protein family A member 1Lepididymis secretory sperm binding protein

Null for drug mechanisms specific to HSPA1L; for Hsp70 family, mechanisms include inhibition of chaperone activity or ATPase cycle, promotion of protein degradation, and modulation of immune response[5]