Next Article in Journal
Biological Functions and Analytical Strategies of Sialic Acids in Tumor
Next Article in Special Issue
Extracellular Matrix Structure and Composition in the Early Four-Chambered Embryonic Heart
Previous Article in Journal
Cytokinesis in Eukaryotic Cells: The Furrow Complexity at a Glance
Previous Article in Special Issue
Fibronectin and Periostin as Prognostic Markers in Ovarian Cancer
Open AccessArticle

HSP90 Interacts with the Fibronectin N-terminal Domains and Increases Matrix Formation

1
Biomedical Biotechnology Research Unit, Department of Biochemistry and Microbiology, Rhodes University, Grahamstown 6140, South Africa
2
Centre for Chemico- and Biomedicinal Research, Rhodes University, Grahamstown 6140, South Africa
*
Author to whom correspondence should be addressed.
Cells 2020, 9(2), 272; https://doi.org/10.3390/cells9020272
Received: 20 December 2019 / Revised: 15 January 2020 / Accepted: 18 January 2020 / Published: 22 January 2020
(This article belongs to the Special Issue Fibronectin in Health and Diseases)
Heat shock protein 90 (HSP90) is an evolutionarily conserved chaperone protein that controls the function and stability of a wide range of cellular client proteins. Fibronectin (FN) is an extracellular client protein of HSP90, and exogenous HSP90 or inhibitors of HSP90 alter the morphology of the extracellular matrix. Here, we further characterized the HSP90 and FN interaction. FN bound to the M domain of HSP90 and interacted with both the open and closed HSP90 conformations; and the interaction was reduced in the presence of sodium molybdate. HSP90 interacted with the N-terminal regions of FN, which are known to be important for matrix assembly. The highest affinity interaction was with the 30-kDa (heparin-binding) FN fragment, which also showed the greatest colocalization in cells and accommodated both HSP90 and heparin in the complex. The strength of interaction with HSP90 was influenced by the inherent stability of the FN fragments, together with the type of motif, where HSP90 preferentially bound the type-I FN repeat over the type-II repeat. Exogenous extracellular HSP90 led to increased incorporation of both full-length and 70-kDa fragments of FN into fibrils. Together, our data suggested that HSP90 may regulate FN matrix assembly through its interaction with N-terminal FN fragments. View Full-Text
Keywords: HSP90; fibronectin; extracellular matrix; client protein; fibrillogenesis HSP90; fibronectin; extracellular matrix; client protein; fibrillogenesis
Show Figures

Figure 1

MDPI and ACS Style

Chakraborty, A.; Boel, N. .-E.; Edkins, A.L. HSP90 Interacts with the Fibronectin N-terminal Domains and Increases Matrix Formation. Cells 2020, 9, 272.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop