Human HSPA9 (mtHsp70, mortalin) interacts with lipid bilayers containing cardiolipin, a major component of the inner mitochondrial membrane

Dores-Silva, Paulo R.; Cauvi, David M.; Kiraly, Vanessa Thomaz Rodrigues; Borges, Júlio César; Maio, Antonio De

doi:10.1016/j.bbamem.2020.183436

Cited by 13 publications

(26 citation statements)

References 73 publications

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“…The recombinant proteins were expressed as previously described (Borges and Ramos 2006;Dores-Silva et al 2020a, 2020bMinari et al 2019). The recombinant proteins were isolated by a single chromatographic step on a Ni 2+immobilized affinity column, step-washed with 20 mM phosphate buffer (pH 7.5) containing 100 mM NaCl.…”

Section: Protein Expression and Purificationmentioning

confidence: 99%

“…Liposomes were prepared using the extrusion method (Lopez et al 2016;Dores-Silva et al 2020a, 2020b.…”

Section: Liposome Preparation and Incorporation Of Proteinsmentioning

confidence: 99%

“…The interaction of HSPA8 with POPS and CL liposomes was assessed by isothermal titration calorimetry (ITC) using an iTC200 microcalorimeter (GE Healthcare Life Sciences) as previously described by Dores-Silva et al 2020a andDores-Silva et al 2020b. Briefly, seventeen aliquots of 2 μL of liposomes (POPS or CL) at 3 mM were titrated into 203.8 μL of 10 μM of HSPA8 at 25°C.…”

Section: Isothermal Titration Calorimetrymentioning

confidence: 99%

“…Previous studies showed that various members of the HSP70 family interacted with high selectively for liposomes made with negatively charged phospholipids (Arispe et al 2004;Schilling et al 2009;Armijo et al 2014;Dores-Silva et al 2020a, 2020b. We investigated whether HSPA8 displays a similar interaction with phospholipid bilayers.…”

Section: Hspa8 Interacts Preferentially With Liposomes Made With Pops or CLmentioning

confidence: 99%

“…Previous studies have shown that the association and insertion of HSP70 into membranes is a complex process that is initiated by the interaction with negatively charged phospholipids that is likely followed by a conformational change permitting the penetration into the core of the lipid bilayer (De Maio 2011;Armijo et al 2014). The insertion of HSP70 into membranes is a spontaneous process due to increases in entropy, likely due to the displacement of water molecules from the surface of the protein (Dores-Silva et al 2020a, 2020b. Human 71 kDa heat shock cognate protein (HSC70, also known as HSPA8, Hsp70-8, Hsc71, Hsp71, or Hsp73), which is constitutively present in cells participating in the folding of newly synthesized polypeptides as well as other specific functions, including endocytosis, was found to get inserted into lipid bilayers opening an ion conductance pathway (Arispe and De Maio 2000;Macazo and White 2014).…”

Section: Introductionmentioning

confidence: 99%

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Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes

Dores-Silva

Cauvi²,

Coto

et al. 2021

Cell Stress and Chaperones

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Heat shock proteins (HSP) are critical elements for the preservation of cellular homeostasis by participating in an array of biological processes. In addition, HSP play an important role in cellular protection from various environmental stresses. HSP are part of a large family of different molecular mass polypeptides, displaying various expression patterns, subcellular localizations, and diversity functions. An unexpected observation was the detection of HSP on the cell surface. Subsequent studies have demonstrated that HSP have the ability to interact and penetrate lipid bilayers by a process initiated by the recognition of phospholipid heads, followed by conformational changes, membrane insertion, and oligomerization. In the present study, we described the interaction of HSPA8 (HSC70), the constitutive cytosolic member of the HSP70 family, with lipid membranes. HSPA8 showed high selectivity for negatively charged phospholipids, such as phosphatidylserine and cardiolipin, and low affinity for phosphatidylcholine. Membrane insertion was mediated by a spontaneous process driven by increases in entropy and diminished by the presence of ADP or ATP. Finally, HSPA8 was capable of driving into the lipid bilayer HSP90 that does not display any lipid biding capacity by itself. This observation suggests that HSPA8 may act as a membrane chaperone.

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Section: Protein Expression and Purificationmentioning

confidence: 99%

“…Liposomes were prepared using the extrusion method (Lopez et al 2016;Dores-Silva et al 2020a, 2020b.…”

Section: Liposome Preparation and Incorporation Of Proteinsmentioning

confidence: 99%

Section: Isothermal Titration Calorimetrymentioning

confidence: 99%

Section: Hspa8 Interacts Preferentially With Liposomes Made With Pops or CLmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes

Dores-Silva

Cauvi²,

Coto

et al. 2021

Cell Stress and Chaperones

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Heat shock proteins and the biogenesis of cellular membranes

Maio

Hightower

2021

Cell Stress and Chaperones

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The interaction of heat shock proteins with cellular membranes: a historical perspective

Maio

Hightower

2021

Cell Stress and Chaperones

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The interaction of heat shock proteins (HSP) with cellular membranes has been an enigmatic process, initially observed by morphological studies, inferred during the purification of HSP70s, and confirmed after the detection of these proteins on the surface of cancer cells and their insertion into artificial lipid bilayers. Today, the association of several HSP with lipid membranes is well established. However, the mechanisms for membrane insertion have been elusive. There is conclusive evidence indicating that HSP70s have a great selectivity for negatively charged phospholipids, whereas other HSP have a broader spectrum of lipid specificity. HSP70 also oligomerizes upon membrane insertion, forming ion conductance channels. The functional role of HSP70 lipid interactions appears related to membrane stabilization that may play a role during cell membrane biogenesis. They could also play a role as membrane chaperones as well as during endocytosis, microautophagy, and signal transduction. Moreover, HSP membrane association is a key component in the extracellular export of these proteins. The presence of HSP70 on the surface of cancer cells and its interaction with lysosome membranes have been envisioned as potential therapeutic targets. Thus, the biology and function of HSP membrane association are reaching a new level of excitement. This review is an attempt to preserve the recollection of the pioneering contributions of many investigators that have participated in this endeavor.

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Human HSPA9 (mtHsp70, mortalin) interacts with lipid bilayers containing cardiolipin, a major component of the inner mitochondrial membrane

Cited by 13 publications

References 73 publications

Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes

Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes

Heat shock proteins and the biogenesis of cellular membranes

The interaction of heat shock proteins with cellular membranes: a historical perspective

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