HSP90 interacts with the fibronectin N-terminal domains and increases matrix formation:

Title: HSP90 interacts with the fibronectin N-terminal domains and increases matrix formation:
Creator: Chakraborty, Abir, Boel, Natasha M-E, Edkins, Adrienne L
Date: 2020
Type: text
Type: article
Identifier: http://hdl.handle.net/10962/165407
Identifier: vital:41241
Identifier: https://doi.org/10.3390/cells9020272
Description: 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.
Format: 27 pages, pdf
Language: English
Relation: Cells, Chakraborty, A., Boel, N.M.E. and Edkins, A.L., 2020. HSP90 interacts with the fibronectin N-terminal domains and increases matrix formation. Cells, 9(2), p.272, Cells volume 9 number 2 1 26 January 2020 2073-4409
Rights: Publisher
Rights: Use of this resource is governed by the terms and conditions of the MDPI Open Access Statement (https://www.int-res.com/journals/terms-of-use/)

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