Characterization of Molecular Interactions of Mytilus edulis Foot Proteins on Model Hydrated Surfaces

Mortalin/mtHsp70 (mitochondrial Hsp70) and HSP60 (heat-shock protein 60) are heat-shock proteins that reside in multiple subcellular compartments, with mitochondria being the predominant one. In the present study, we demonstrate that the two proteins interact both in vivo and in vitro, and that the N-terminal region of mortalin is involved in these interactions. Suppression of HSP60 expression by shRNA (short hairpin RNA) plasmids caused the growth arrest of cancer cells similar to that obtained by suppression of mortalin expression by ribozymes. An overexpression of mortalin, but not of HSP60, extended the in vitro lifespan of normal fibroblasts (TIG-1). Taken together, this study for the first time delineates: (i) molecular interactions of HSP60 with mortalin; (ii) their co- and exclusive localizations in vivo; (iii) their involvement in tumorigenesis; and (iv) their functional distinction in pathways involved in senescence.

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Interfacial characterization of the molecular interactions in mixed monolayers of coumarin and phospholipids

Journal of King Saud University - Science ◽

10.1016/j.jksus.2018.05.020 ◽

2019 ◽

Vol 31 (4) ◽

pp. 452-459 ◽

Cited By ~ 2

Author(s):

Felipe S. Rocha ◽

Gustavo S. Codeceira ◽

Maria D.L. Oliveira ◽

Cesar A.S. Andrade

Keyword(s):

Molecular Interactions ◽

Mixed Monolayers

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Characterization of distinct molecular interactions responsible for IRF3 and IRF7 phosphorylation and subsequent dimerization

Nucleic Acids Research ◽

10.1093/nar/gkaa873 ◽

2020 ◽

Vol 48 (20) ◽

pp. 11421-11433

Author(s):

Louise Dalskov ◽

Ryo Narita ◽

Line L Andersen ◽

Nanna Jensen ◽

Sonia Assil ◽

...

Keyword(s):

Immune Response ◽

Transcription Factors ◽

Molecular Interactions ◽

Adaptor Proteins ◽

Innate Immune ◽

Charged Surface ◽

Regulatory Domain ◽

Phosphorylation Event ◽

Positively Charged

Abstract IRF3 and IRF7 are critical transcription factors in the innate immune response. Their activation is controlled by phosphorylation events, leading to the formation of homodimers that are transcriptionally active. Phosphorylation occurs when IRF3 is recruited to adaptor proteins via a positively charged surface within the regulatory domain of IRF3. This positively charged surface also plays a crucial role in forming the active homodimer by interacting with the phosphorylated sites stabilizing the homodimer. Here, we describe a distinct molecular interaction that is responsible for adaptor docking and hence phosphorylation as well as a separate interaction responsible for the formation of active homodimer. We then demonstrate that IRF7 can be activated by both MAVS and STING in a manner highly similar to that of IRF3 but with one key difference. Regulation of IRF7 appears more tightly controlled; while a single phosphorylation event is sufficient to activate IRF3, at least two phosphorylation events are required for IRF7 activation.

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