HSPA8

Case study 1: Lei Wang, 2022

Porcine reproductive and respiratory syndrome virus (PRRSV), a porcine arterivirus, causes severe financial losses to global swine industry. Despite much research, the molecular mechanisms of PRRSV infection remains to be fully elucidated.

In this study, the researchers uncovered the involvement of heat shock protein member 8 (HSPA8) in PRRSV attachment and internalization during infection for the first time. In detail, HSPA8 was identified to interact with PRRSV glycoprotein 4 (GP4). Chemical inhibitors and specific small interference RNAs (siRNAs) targeting HSPA8 significantly suppressed PRRSV infection as indicated by decreased viral RNA abundance, infectivity, and titers. these results demonstrate that HSPA8 is important for PRRSV attachment and internalization, which is a potential target to prevent and control the viral infection.

Fig1. GP4-mCherry co-localized with endogenous HSPA8. HEK-293T cells were transfected with the plasmid expressing GP4-mCherry (red) or mCherry (red) for 24 h, and stained with anti-HSPA8 pAbs.

Fig2. HSPA8 PB domain interacted with GP4-mCherry.

Case study 2: Riccardo Sirtori, 2020

Heat shock protein 70 family was demonstrated to play a critical role in protein homeostasis, a process profoundly impaired in neurodegenerative disorders. Neurodegenerative diseases are characterized by the accumulation of different kind of proteins and the formation of insoluble aggregates which are toxic for neurons. To explore the role of heat shock protein family 70 (in particular HSPA8 and HSPA1A) in the accumulation of proteins implied in neurodegeneration pathogenesis, in this study the researchers verified in human SH-SY5Y neuroblastoma cells how HSPA8 or HSPA1A knock-down can affect protein levels of tau, superoxide dismutase 1 and α-synuclein. The results suggest HSPA8 can play an important role in the homeostasis of tau, superoxide dismutase 1 and α-synuclein and in the balance between α-synuclein oligomeric and monomeric forms.

Fig3. siRNA-mediated knock-down of HSPA8 and HSPA1A in SH-SY5Y cell line. Relative protein levels of HSPA8 and HSPA1A after silencing of HSPA8 or HSPA1A.

Fig4. Representative Western blot images in SH-SY5Y knocked-down for HSPA8 or HSPA1A.

Fig1. Model depicts the involvement of HSPA8 in PRRSV attachment and internalization. HSPA8 functions as a co-factor for PRRSV infection. (Lei Wang, 2022)

Fig2. Proposed model for HSC70-mediated Golgi association of ARL5B. (Ebsy Jaimon, 2021)

HSPA8 involved in several pathways and played different roles in them. We selected most pathways HSPA8 participated on our site, such as Spliceosome, MAPK signaling pathway, Protein processing in endoplasmic reticulum, which may be useful for your reference. Also, other proteins which involved in the same pathway with HSPA8 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

HSPA8 has several biochemical functions, for example, ATP binding, ATPase activity, ATPase activity, coupled. Some of the functions are cooperated with other proteins, some of the functions could acted by HSPA8 itself. We selected most functions HSPA8 had, and list some proteins which have the same functions with HSPA8. You can find most of the proteins on our site.

HSPA8 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with HSPA8 here. Most of them are supplied by our site. Hope this information will be useful for your research of HSPA8.

STUB1; LRRK2; HSPBP1; EGFR