Ong M.S.Deng S.Halim C.E.Cai W.Tan T.Z.RUBY YUN-JU HUANGSethi G.Hooi S.C.Kumar A.P.Yap C.T.2020-06-262020-06-2620202072-6694https://www.scopus.com/inward/record.uri?eid=2-s2.0-85079184412&doi=10.3390%2fcancers12010238&partnerID=40&md5=2b70e8abe98a3c2bb53408ea3d26ae82https://scholars.lib.ntu.edu.tw/handle/123456789/504710Cytoskeletal proteins, which consist of different sub-families of proteins including microtubules, actin and intermediate filaments, are essential for survival and cellular processes in both normal as well as cancer cells. However, in cancer cells, these mechanisms can be altered to promote tumour development and progression, whereby the functions of cytoskeletal proteins are co-opted to facilitate increased migrative and invasive capabilities, proliferation, as well as resistance to cellular and environmental stresses. Herein, we discuss the cytoskeletal responses to important intracellular stresses (such as mitochondrial, endoplasmic reticulum and oxidative stresses), and delineate the consequences of these responses, including effects on oncogenic signalling. In addition, we elaborate how the cytoskeleton and its associated molecules present themselves as therapeutic targets. The potential and limitations of targeting new classes of cytoskeletal proteins are also explored, in the context of developing novel strategies that impact cancer progression. ? 2020 by the authors. Licensee MDPI, Basel, Switzerland.Cancer; Cytoskeletal molecules; Endoplasmic reticulum stress; Mitochondrial stress; Oxidative stress; Therapeutics[SDGs]SDG31 ethyl 2 [[3 ethyl 5 (3 methylbenzothiazolin 2 ylidene) 4 oxothiazolidin 2 ylidene]methyl]pyridinium chloride; abituzumab; actin; cytochalasin; cytoskeleton protein; docetaxel; dynamin; dynamin related protein 1; epothilone derivative; gelsolin; histone deacetylase 6; histone deacetylase inhibitor; integrin; ixabepilone; jaspamide; LIM kinase; mitofusin 1; mitofusin 2; paclitaxel; proteasome inhibitor; salinomycin; silibinin; taxane derivative; tubacin; tubulin; unclassified drug; vimentin; Vinca alkaloid; voltage dependent anion channel; withaferin A; antiproliferative activity; cancer chemotherapy; cancer growth; cancer inhibition; cancer resistance; carcinogenesis; castration resistant prostate cancer; cell stress; DNA damage; drug potentiation; drug targeting; endoplasmic reticulum stress; epithelial mesenchymal transition; human; metastatic colorectal cancer; microfilament; microtubule; mitochondrial dynamics; mitochondrial fission; mitochondrial fusion; mitophagy; multiple myeloma; nonhuman; oxidative stress; proapoptotic activity; Review; signal transduction; tumor regressionreview10.3390/cancers120102382-s2.0-85079184412