Heat shock protein family B member 2 (HSPB2)

Heat shock protein family B member 2 (HSPB2) is a small heat-shock protein with a conserved α-crystallin domain and is predominantly expressed in heart and skeletal muscle. It acts as a molecular chaperone, preventing protein aggregation and assisting in protein folding during stress conditions. HSPB2 specifically binds to and activates the myotonic dystrophy protein kinase (DMPK), playing crucial roles in muscle structure maintenance and function. While HSPB2 is not heat-inducible, it participates broadly in cytoprotection, protein quality control, and cellular homeostasis, and is implicated in cardiac, muscular, and neurodegenerative diseases, often elevated in disease states as a compensatory response[1][2][3][4][6]. No clinically relevant small molecule or biologic drugs are known to selectively target HSPB2, and its primary recognized function is as a molecular chaperone—not a receptor, enzyme, or transporter.

Other names

Heat shock protein beta-2HspB2MKBPMyotonic dystrophy kinase-binding proteinDMPK-binding proteinheat shock 27kDa protein 2LOH11CR1K