Stip1 Gene is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
STIP1 (Stress-Induced Phosphoprotein 1), also known as Hsp70/Hsp90 Organizing Protein (HOP), is a co-chaperone protein that bridges Hsp70 and Hsp90 molecular chaperones. STIP1 plays a crucial role in facilitating protein folding, assembly of protein complexes, and regulation of signaling pathways. It is essential for the proper function of the Hsp90 chaperone system, which is critical for folding many client proteins involved in neurodegeneration [1][2].
| Property | Value |
|---|---|
| Protein Name | STIP1 / HOP |
| Gene | STIP1 |
| UniProt ID | Q9YLS8 |
| Molecular Weight | ~62.5 kDa (548 amino acids) |
| Aliases | HOP, Hsp70/Hsp90 Organizer, STI1 |
| Tissue Specificity | Ubiquitous, high in brain |
STIP1 contains multiple functional domains:
STIP1 serves as a molecular adaptor:
STIP1 participates in:
In the nervous system:
STIP1 in AD:
In PD:
STIP1 is often overexpressed in cancers:
Key STIP1 interactions:
Targeting STIP1:
The study of Stip1 Gene has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.
Blatch GL, et al. (1997). The Hsp70-Hsp90 co-chaperone Hop. Biol Chem. 378(7):661-669. PMID:9257423 ↩︎
Young JC, et al. (1998). Hsp70 chaperone systems: diversity of cellular functions. J Cell Sci. 111 ( Pt 1):1-10. PMID:9434029 ↩︎
Scheufler C, et al. (2000). Structure of TPR domain-peptide complexes: identification of common themes in co-chaperone interactions. Cell. 101(2):201-210. PMID:10786833 ↩︎
Johnson BD, et al. (1998). Hop modulates Hsp70/Hsp90 interactions in protein folding. J Biol Chem. 273(6):3679-3686. PMID:9452489 ↩︎
Pratt WB, et al. (2010). Targeting the Hsp90-associated proteostasis. Annu Rev Pharmacol Toxicol. 50:111-132. PMID:20055701 ↩︎
Tutar L, et al. (2006). Hsp90 and neurodegeneration. Adv Exp Med Biol. 594:107-117. PMID:17075914 ↩︎
Opattova A, et al. (2015). The Hsp90 chaperone as a therapeutic target in neurodegenerative diseases. Int J Mol Sci. 16(10):24486-24497. PMID:26540057 ↩︎
Daturpalli S, et al. (2013). Hsp90 inhibition reduces aggregation of a synuclein. J Mol Biol. 425(22):4614-4628. PMID:23933087 ↩︎
Song X, et al. (2017). STIP1 is overexpressed in cancer and promotes tumor growth. Oncotarget. 8(40):67782-67793. PMID:28978095 ↩︎