Biography
Dr Pat Kiely is a Lecturer in the Department of Life Sciences, Principal Investigator of the Laboratory of Cellular and Molecular Biology, and member of the Materials and Surface Science Institute and Stokes Institute. Dr Kiely has a BSc. in Biomedical Science and a PhD in Biochemistry from University College Cork. Dr Kiely's work has led to a number of significant publications which were the foundation to the acquisition of several prestigious postdoctoral fellowships and international awards including European Association for Cancer Research (EACR) Young Scientist Award (2010), The Irish Cancer Society Research Fellowship (2009), The Roche Gold Medal' for Postdoctoral researcher of the year (2007), The Pfizer Gold medal for Excellence in Research' in 2007 and 2002, Career Development Fellowship (HRB, 2005) and Young Investigator of the Year 2006', awarded by the Biochemical Society, UK.
Research Interests:
The research emphasis in my laboratory is on deciphering the localized and transient signalling events which occur in cells during migration. Cell migration is orchestrated by a series of complex signalling cascades which requires crosstalk between cell surface receptors and components of the cell cytoskeleton. Understanding the molecular mechanisms that regulate cell migration is of important intellectual and clinical interest, and we believe this work may reveal fresh approaches to target cancer as well as developmental and neurodegenerative diseases.
Research projects ongoing in the laboratory range from the most fundamental, where the development of a better understanding of the molecular mechanism(s) regulating cell migration is the goal, to the very applied, where the identification of novel therapeutic targets and the design and synthesis of novel materials and surfaces to study cell behavior is the desired endpoint. To help us achieve our goals, we are using a series of complimentary and synergistic cellular and molecular approaches and novel technologies including: 3D cell culture models, neuronal models, 2D ESI MS/MS, peptide array technology, interferometry, label free live cell monitoring, qPCR and droplet qPCR, SEM, TEM, con-focal microscopy, and electro spinning of materials. In collaboration with Dr Tara Daltons group (Stokes Institute) we are applying novel gene expression techniques and droplet technology to decipher signaling pathways in breast and colon cancer.
Research Interests
Publications
Book Chapters
The IGF-1 Receptor in Cells Survival: Signalling and Regulation.
P.A. Kiely, D.M. O'Gorman, A. Lyons, R. O'Connor
(2004)
The IGF-1 Receptor in Cells Survival: Signalling and Regulation.
In Cell Engineering;
Kluwer :
Springer
Peer Reviewed Journals
RACK1 promotes neurite outgrowth by scaffolding AGAP2 to FAK
Dwane, S,Durack, E,O'Connor, R,Kiely, PA
(2014)
RACK1 promotes neurite outgrowth by scaffolding AGAP2 to FAK
In Cellular signalling;
pp. 9-18
DOI: 10.1016/j.cellsig.2013.08.036
Inhibition of transcription by B Cell Leukaemia 3 (Bcl-3) requires interaction with Nuclear Factor (NF)-κB p50.
Collins PE, Kiely PA, Carmody RJ
(2014)
Inhibition of transcription by B Cell Leukaemia 3 (Bcl-3) requires interaction with Nuclear Factor (NF)-κB p50.
In The Journal of biological chemistry;
DOI: 10.1074/jbc.M114.551986
[ULIR]
Deubiquitination of NF-kappa B by Ubiquitin-Specific Protease-7 promotes transcription
Colleran, A,Collins, PE,O'Carroll, C,Ahmed, A,Mao, XC,McManus, B,Kiely, PA,Burstein, E,Carmody, RJ
(2013)
Deubiquitination of NF-kappa B by Ubiquitin-Specific Protease-7 promotes transcription
In Proceedings Of The National Academy Of Sciences Of The United States Of America;
pp. 618-623
DOI: 10.1073/pnas.1208446110
Pregnancy-Specific Glycoproteins Bind Integrin alpha IIb beta 3 and Inhibit the Platelet-Fibrinogen Interaction
Shanley, DK,Kiely, PA,Golla, K,Allen, S,Martin, K,O'Riordan, RT,Ball, M,Aplin, JD,Singer, BB,Caplice, N,Moran, N,Moore, T
(2013)
Pregnancy-Specific Glycoproteins Bind Integrin alpha IIb beta 3 and Inhibit the Platelet-Fibrinogen Interaction
In Plos One;
DOI: 10.1371/journal.pone.0057491
[ULIR]
RACK1 promotes neurite outgrowth by scaffolding AGAP2 to FAK.
Dwane S, Durack E, O'Connor R, Kiely PA
(2013)
RACK1 promotes neurite outgrowth by scaffolding AGAP2 to FAK.
In Cellular signalling;
DOI: 10.1016/j.cellsig.2013.08.036
RACK(1) to the future - a historical perspective
Ron, D,Adams, DR,Baillie, GS,Long, A,O'Connor, R,Kiely, PA
(2013)
RACK(1) to the future - a historical perspective
In Cell Commun Signal;
DOI: 10.1186/1478-811X-11-53
[ULIR]
Dynamic complex formation between HD-GYP, GGDEF and PilZ domain proteins regulates motility in Xanthomonas campestris.
Ryan RP, McCarthy Y, Kiely PA, O'Connor R, Farah CS, Armitage JP, Dow JM
(2012)
Dynamic complex formation between HD-GYP, GGDEF and PilZ domain proteins regulates motility in Xanthomonas campestris.
In Molecular microbiology;
DOI: 10.1111/mmi.12000
Direct interaction between scaffolding proteins RACK1 and 14-3-3ζ regulates brain-derived neurotrophic factor (BDNF) transcription.
Neasta J, Kiely PA, He DY, Adams DR, O'Connor R, Ron D
(2012)
Direct interaction between scaffolding proteins RACK1 and 14-3-3ζ regulates brain-derived neurotrophic factor (BDNF) transcription.
In The Journal of biological chemistry;
pp. 322-336
DOI: 10.1074/jbc.M111.272195
GSK-3β phosphorylation of the IGF-1 Receptor C terminal tail restrains kinase activity and cell growth.
Kelly GM, Buckley DA, Kiely PA, Adams DR, O'Connor R
(2012)
GSK-3β phosphorylation of the IGF-1 Receptor C terminal tail restrains kinase activity and cell growth.
In The Journal of biological chemistry;
DOI: 10.1074/jbc.M112.385757
Tools used to study how protein complexes are assembled in signaling cascades.
Dwane S, Kiely PA
(2011)
Tools used to study how protein complexes are assembled in signaling cascades.
In Bioengineered bugs;
pp. 247-259
DOI: 10.4161/bbug.2.5.17844
RACK1, A multifaceted scaffolding protein: Structure and function.
Adams DR, Ron D, Kiely PA
(2011)
RACK1, A multifaceted scaffolding protein: Structure and function.
In Cell Commun Signal;
DOI: 10.1186/1478-811X-9-22
[ULIR]
Phosphorylation of RACK1 on tyrosine 52 by c-Abl is required for insulin-like growth factor I-mediated regulation of focal adhesion kinase.
Kiely PA, Baillie GS, Barrett R, Buckley DA, Adams DR, Houslay MD, O'Connor R
(2009)
Phosphorylation of RACK1 on tyrosine 52 by c-Abl is required for insulin-like growth factor I-mediated regulation of focal adhesion kinase.
In The Journal of biological chemistry;
pp. 20263-20274
DOI: 10.1074/jbc.M109.017640
Tyrosine 302 in RACK1 is essential for insulin-like growth factor-I-mediated competitive binding of PP2A and beta1 integrin and for tumor cell proliferation and migration.
Kiely PA, Baillie GS, Lynch MJ, Houslay MD, O'Connor R
(2008)
Tyrosine 302 in RACK1 is essential for insulin-like growth factor-I-mediated competitive binding of PP2A and beta1 integrin and for tumor cell proliferation and migration.
In The Journal of biological chemistry;
pp. 22952-22961
DOI: 10.1074/jbc.M800802200
Effects of RACK1 on cell migration and IGF-I signalling in cardiomyoctes are not dependent on an association with the IGF-IR.
O'Donovan HC, Kiely PA, O'Connor R
(2007)
Effects of RACK1 on cell migration and IGF-I signalling in cardiomyoctes are not dependent on an association with the IGF-IR.
In Cellular signalling;
pp. 2588-2595
DOI: 10.1016/j.cellsig.2007.08.010
Insulin-like growth factor I controls a mutually exclusive association of RACK1 with protein phosphatase 2A and beta1 integrin to promote cell migration.
Kiely PA, O'Gorman D, Luong K, Ron D, O'Connor R
(2006)
Insulin-like growth factor I controls a mutually exclusive association of RACK1 with protein phosphatase 2A and beta1 integrin to promote cell migration.
In Molecular and cellular biology;
pp. 4041-4051
DOI: 10.1128/MCB.01868-05
RACK1-mediated integration of adhesion and insulin-like growth factor I (IGF-I) signaling and cell migration are defective in cells expressing an IGF-I receptor mutated at tyrosines 1250 and 1251.
Kiely PA, Leahy M, O'Gorman D, O'Connor R
(2005)
RACK1-mediated integration of adhesion and insulin-like growth factor I (IGF-I) signaling and cell migration are defective in cells expressing an IGF-I receptor mutated at tyrosines 1250 and 1251.
In The Journal of biological chemistry;
pp. 7624-7633
DOI: 10.1074/jbc.M412889200
Gene expression profiles in cells transformed by overexpression of the IGF-I receptor.
Loughran G, Huigsloot M, Kiely PA, Smith LM, Floyd S, Ayllon V, O'Connor R
(2005)
Gene expression profiles in cells transformed by overexpression of the IGF-I receptor.
In Oncogene;
pp. 6185-6193
DOI: 10.1038/sj.onc.1208772
Mystique is a new insulin-like growth factor-I-regulated PDZ-LIM domain protein that promotes cell attachment and migration and suppresses Anchorage-independent growth.
Loughran G, Healy NC, Kiely PA, Huigsloot M, Kedersha NL, O'Connor R
(2005)
Mystique is a new insulin-like growth factor-I-regulated PDZ-LIM domain protein that promotes cell attachment and migration and suppresses Anchorage-independent growth.
In Molecular biology of the cell;
pp. 1811-1822
DOI: 10.1091/mbc.E04-12-1052
RACK1 is an insulin-like growth factor 1 (IGF-1) receptor-interacting protein that can regulate IGF-1-mediated Akt activation and protection from cell death.
Kiely PA, Sant A, O'Connor R
(2002)
RACK1 is an insulin-like growth factor 1 (IGF-1) receptor-interacting protein that can regulate IGF-1-mediated Akt activation and protection from cell death.
In The Journal of biological chemistry;
pp. 22581-22589
DOI: 10.1074/jbc.M201758200
Regulation of insulin-like growth factor type I (IGF-I) receptor kinase activity by protein tyrosine phosphatase 1B (PTP-1B) and enhanced IGF-I-mediated suppression of apoptosis and motility in PTP-1B-deficient fibroblasts.
Buckley DA, Cheng A, Kiely PA, Tremblay ML, O'Connor R
(2002)
Regulation of insulin-like growth factor type I (IGF-I) receptor kinase activity by protein tyrosine phosphatase 1B (PTP-1B) and enhanced IGF-I-mediated suppression of apoptosis and motility in PTP-1B-deficient fibroblasts.
In Molecular and cellular biology;
pp. 1998-2010