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Catherine J Pallen
PhD

Investigator Emeritus, Michael Cuccione Childhood Cancer Research Program, BC Children's Hospital
Scientist, Michael Cuccione Childhood Cancer Research Program
Associate Member, Department of Pathology and Laboratory Medicine, University of British Columbia

Reversible protein tyrosine phosphorylation is a prominent mechanism utilized in controlling these signalling pathways: protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs) co-ordinately determine the tyrosine phosphorylation status and the function of a particular substrate protein. Perturbations of such signalling pathways underlie a variety of pathological conditions. Aberrant tyrosine phosphorylation due to malfunctioning PTKs is well established as the basis of several human diseases, in particular human cancers. It is becoming apparent that defective or deregulated PTPs are likewise critical in the development and progression of some human diseases such as cancer and diabetes. Consequently, PTPs are excellent targets for disease intervention.

Academic Affiliations

  • Professor Emeritus/a, Division of Hematology and Oncology, Department of Pediatrics, Faculty of Medicine, University of British Columbia
  • Research Theme: Childhood Diseases
  • Research Group(s): Childhood Cancer and Blood Research

Contact Information

Location

4500 Oak St, Vancouver, BC, Canada, V6H 3N1

(604) 875-2439

cpallen@mail.ubc.ca

PTPa is required for laminin-2-induced Fyn"Akt signaling to drive oligodendrocyte differentiation

Journal of Cell Science

Philip T. T. Ly and Craig Stewart and Catherine J. Pallen

DOI: 10.1242/jcs.212076

08 / 2018

The Interaction of protein-tyrosine phosphatasea (PTPa) and RACK1 protein enables insulin-like growth factor 1 (IGF-1)-stimulated Abl-dependent and -independent tyrosine phosphorylation of PTPa

Journal of Biological Chemistry

Khanna, R.S. and Le, H.T. and Wang, J. and Fung, T.C.H. and Pallen, C.J.

DOI: 10.1074/jbc.M114.624247

Protein Tyrosine Phosphatases in Mast Cell Signaling

Mast Cells

Alexander Geldman and Catherine J. Pallen

DOI: 10.1007/978-1-4939-1568-2_17

09 / 2014

Tyrosine phosphatase PTPa contributes to HER2-evoked breast tumor initiation and maintenance

Oncogene

Meyer, D.S. and Aceto, N. and Sausgruber, N. and Brinkhaus, H. and Mller, U. and Pallen, C.J. and Bentires-Alj, M.

DOI: 10.1038/onc.2012.585

Grb2 Promotes Integrin-Induced Focal Adhesion Kinase (FAK) Autophosphorylation and Directs the Phosphorylation of Protein Tyrosine Phosphatase by the Src-FAK Kinase Complex

Molecular and Cellular Biology

S. Y. S. Cheng and G. Sun and D. D. Schlaepfer and C. J. Pallen

DOI: 10.1128/mcb.00825-13

11 / 2013

TDP1 and PARP1 Deficiency Are Cytotoxic to Rhabdomyosarcoma Cells

Molecular Cancer Research

H. K. Fam and C. Walton and S. A. Mitra and M. Chowdhury and N. Osborne and K. Choi and G. Sun and P. C. W. Wong and M. J. O'Sullivan and G. Turashvili and S. Aparicio and T. J. Triche and M. Bond and C. J. Pallen and C. F. Boerkoel

DOI: 10.1158/1541-7786.mcr-12-0575

08 / 2013

Protein Tyrosine Phosphatase Phosphotyrosyl-789 Binds BCAR3 To Position Cas for Activation at Integrin-Mediated Focal Adhesions

Molecular and Cellular Biology

G. Sun and S. Y. S. Cheng and M. Chen and C. J. Lim and C. J. Pallen

DOI: 10.1128/mcb.00214-12

07 / 2012

Loss of Protein-tyrosine Phosphatase a (PTPa) Increases Proliferation and Delays Maturation of Oligodendrocyte Progenitor Cells

Journal of Biological Chemistry

P.-S. Wang and J. Wang and Y. Zheng and C. J. Pallen

DOI: 10.1074/jbc.m111.312769

02 / 2012

Receptor-like Protein-tyrosine Phosphatase Enhances Cell Surface Expression of Neural Adhesion Molecule NB-3

Journal of Biological Chemistry

H. Ye and T. Zhao and Y. L. J. Tan and J. Liu and C. J. Pallen and Z.-C. Xiao

DOI: 10.1074/jbc.m110.214080

05 / 2011

YB-1 bridges neural stem cells and brain tumor-initiating cells via its roles in differentiation and cell growth

Cancer Research

Fotovati, A. and Abu-Ali, S. and Wang, P.-S. and Deleyrolle, L.P. and Lee, C. and Triscott, J. and Chen, J.Y. and Franciosi, S. and Nakamura, Y. and Sugita, Y. and Uchiumi, T. and Kuwano, M. and Leavitt, B.R. and Singh, S.K. and Jury, A. and Jones, C. and Wakimoto, H. and Reynolds, B.A. and Pallen, C.J. and Dunn, S.E.

DOI: 10.1158/0008-5472.CAN-10-2805

PTPa activates Lyn and Fyn and suppresses Hck to negatively regulate FceRI-dependent mast cell activation and allergic responses

Journal of Immunology

Samayawardhena, L.A. and Pallen, C.J.

DOI: 10.4049/jimmunol.1001261

Small interfering RNA library screen of human kinases and phosphatases identifies polo-like kinase 1 as a promising new target for the treatment of pediatric rhabdomyosarcomas

Molecular Cancer Therapeutics

K. Hu and C. Lee and D. Qiu and A. Fotovati and A. Davies and S. Abu-Ali and D. Wai and E. R. Lawlor and T. J. Triche and C. J. Pallen and S. E. Dunn

DOI: 10.1158/1535-7163.mct-09-0365

11 / 2009

Protein-tyrosine Phosphatase Acts as an Upstream Regulator of Fyn Signaling to Promote Oligodendrocyte Differentiation and Myelination

Journal of Biological Chemistry

P.-S. Wang and J. Wang and Z.-C. Xiao and C. J. Pallen

DOI: 10.1074/jbc.m109.061770

10 / 2009

Protein tyrosine phosphatase-a complexes with the IGF-I receptor and undergoes IGF-I-stimulated tyrosine phosphorylation that mediates cell migration

American Journal of Physiology - Cell Physiology

Chen, S.C. and Khanna, R.S. and Bessette, D.C. and Samayawardhena, L.A. and Pallen, C.J.

DOI: 10.1152/ajpcell.00110.2009

Protein-tyrosine Phosphatase Regulates Stem Cell Factor-dependent c-Kit Activation and Migration of Mast Cells

Journal of Biological Chemistry

L. A. Samayawardhena and C. J. Pallen

DOI: 10.1074/jbc.m804077200

08 / 2008

Breaking the pain connection

Nature Medicine

Pallen, C.J.

DOI: 10.1038/nm1208-1313

Neural recognition molecules CHL1 and NB-3 regulate apical dendrite orientation in the neocortex via PTPa

EMBO Journal

Ye, H. and Tan, Y.L.J. and Ponniah, S. and Takeda, Y. and Wang, S.-Q. and Schachner, M. and Watanabe, K. and Pallen, C.J. and Xiao, Z.-C.

DOI: 10.1038/sj.emboj.7601939

Distinct FAK-Src activation events promote a51 and a41 integrin-stimulated neuroblastoma cell motility

Oncogene

Wu, L. and Bernard-Trifilo, J.A. and Lim, Y. and Lim, S.-T. and Mitra, S.K. and Uryu, S. and Chen, M. and Pallen, C.J. and Cheung, N.-K.V. and Mikolon, D. and Mielgo, A. and Stupack, D.G. and Schlaepfer, D.D.

DOI: 10.1038/sj.onc.1210770

PRL PTPs: Mediators and markers of cancer progression

Cancer and Metastasis Reviews

Bessette, D.C. and Qiu, D. and Pallen, C.J.

DOI: 10.1007/s10555-008-9121-3

Differential Function of PTP and PTP Y789F in T Cells and Regulation of PTP Phosphorylation at Tyr-789 by CD45

Journal of Biological Chemistry

L. Maksumova and Y. Wang and N. K. Y. Wong and H. T. Le and C. J. Pallen and P. Johnson

DOI: 10.1074/jbc.m703157200

05 / 2007

Ewing sarcoma with novel translocation t(2;16) producing an in-flame fusion of FUS and FEV

Journal of Molecular Diagnostics

Ng, T.L. and O'Sullivan, M.J. and Pallen, C.J. and Hayes, M. and Clarkson, P.W. and Winstanley, M. and Sorensen, P.H.B. and Nielsen, T.O. and Horsman, D.E.

DOI: 10.2353/jmoldx.2007.070009

PRL-3: A metastasis-associated phosphatase in search of a function

Cells Tissues Organs

Bessette, D.C. and Wong, P.C.W. and Pallen, C.J.

DOI: 10.1159/000101324

Integrin-induced Tyrosine Phosphorylation of Protein-tyrosine Phosphatase- Is Required for Cytoskeletal Reorganization and Cell Migration

Journal of Biological Chemistry

M. Chen and S. C. Chen and C. J. Pallen

DOI: 10.1074/jbc.m600561200

02 / 2006

Reduced NMDA receptor tyrosine phosphorylation in PTPa-deficient mouse synaptosomes is accompanied by inhibition of four src family kinases and Pyk2: An upstream role for PTPa in NMDA receptor regulation

Journal of Neurochemistry

Le, H.T. and Maksumova, L. and Wang, J. and Pallen, C.J.

DOI: 10.1111/j.1471-4159.2006.04075.x

Differential effects of interleukin-1 and transforming growth factor-1 on the expression of the inflammation-associated protein, ADAMTS-1, in human decidual stromal cells in vitro

Human Reproduction

Ng, Y.H. and Zhu, H. and Pallen, C.J. and Leung, P.C.K. and MacCalman, C.D.

DOI: 10.1093/humrep/del108

Akt phosphorylates the Y-box binding protein 1 at Ser102 located in the cold shock domain and affects the anchorage-independent growth of breast cancer cells

Oncogene

Sutherland, B.W. and Kucab, J. and Wu, J. and Lee, C. and Cheang, M.C.U. and Yorida, E. and Turbin, D. and Dedhar, S. and Nelson, C. and Pollak, M. and Grimes, H.L. and Miller, K. and Badve, S. and Huntsman, D. and Blake-Gilks, C. and Chen, M. and Pallen, C.J. and Dunn, S.E.

DOI: 10.1038/sj.onc.1208590

Protein tyrosine phosphatase a regulates Fyn activity and Cbp/PAG phosphorylation in thymocyte lipid rafts

Journal of Immunology

Maksumova, L. and Le, H.T. and Muratkhodjaev, F. and Davidson, D. and Veillette, A. and Pallen, C.J.

Insulin signaling and glucose homeostasis in mice lacking protein tyrosine phosphatase a

Biochemical and Biophysical Research Communications

Le, H.T. and Ponniah, S. and Pallen, C.J.

DOI: 10.1016/j.bbrc.2003.12.087

Protein Tyrosine Phosphatase α (PTPα): A Src Family Kinase Activator and Mediator of Multiple Biological Effects

CTMC

Catherine Pallen

DOI: 10.2174/1568026033452320

03 / 2003

Protein tyrosine phosphatase alpha (PTPalpha): a Src family kinase activator and mediator of multiple biological effects.

Current topics in medicinal chemistry

Pallen, C.J.

Protein tyrosine phosphatase alpha (PTPa) knockout mice show deficits in Morris water maze learning, decreased locomotor activity, and decreases in anxiety

Brain Research

Skelton, M.R. and Ponniah, S. and Wang, D.Z.-M. and Doetschman, T. and Vorhees, C.V. and Pallen, C.J.

DOI: 10.1016/S0006-8993(03)02839-7

PRL-3 and PRL-1 promote cell migration, invasion, and metastasis

Cancer Research

Zeng, Q. and Dong, J.-M. and Guo, K. and Li, J. and Tan, H.-X. and Koh, V. and Pallen, C.J. and Manser, E. and Hong, W.

Nogo-A at CNS paranodes is a ligand of Caspr: Possible regulation of K + channel localization

EMBO Journal

Nie, D.-Y. and Zhou, Z.-H. and Ang, B.-T. and Teng, F.Y.H. and Xu, G. and Xiang, T. and Wang, C.-Y. and Zeng, L. and Takeda, Y. and Xu, T.-L. and Ng, Y.-K. and Faivre-Sarrailh, C. and Popko, B. and Ling, E.-A. and Schachner, M. and Watanabe, K. and Pallen, C.J. and Tang, B.L. and Xiao, Z.-C.

DOI: 10.1093/emboj/cdg570

PTPa regulates integrin-stimulated FAK autophosphorylation and cytoskeletal rearrangement in cell spreading and migration

Journal of Cell Biology

Zeng, L. and Si, X. and Yu, W.-P. and Thi Le, H. and Ng, K.P. and Teng, R.M.H. and Ryan, K. and Wang, D.Z.-M. and Ponniah, S. and Pallen, C.J.

DOI: 10.1083/jcb.200206049

F3/contactin acts as a functional ligand for notch during oligodendrocyte maturation

Cell

Hu, Q.-D. and Ang, B.-T. and Karsak, M. and Hu, W.-P. and Cui, X.-Y. and Duka, T. and Takeda, Y. and Chia, W. and Sankar, N. and Ng, Y.-K. and Ling, E.-A. and Maciag, T. and Small, D. and Trifonova, R. and Kopan, R. and Okano, H. and Nakafuku, M. and Chiba, S. and Hirai, H. and Aster, J.C. and Schachner, M. and Pallen, C.J. and Watanabe, K. and Xiao, Z.-C.

DOI: 10.1016/S0092-8674(03)00810-9

Interaction of Farnesylated PRL-2, a Protein-tyrosine Phosphatase, with the -Subunit of Geranylgeranyltransferase II

Journal of Biological Chemistry

X. Si and Q. Zeng and C. H. Ng and W. Hong and C. J. Pallen

DOI: 10.1074/jbc.m010400200

07 / 2001

Conserved synteny between the Fugu and human PTEN locus and the evolutionary conservation of vertebrate PTEN function

Oncogene

Yu, W.-P. and Pallen, C.J. and Tay, A. and Jirik, F.R. and Brenner, S. and Tan, Y.H. and Venkatesh, B.

DOI: 10.1038/sj.onc.1204679

Calmodulin Binds to and Inhibits the Activity of the Membrane Distal Catalytic Domain of Receptor Protein-tyrosine Phosphatase

Journal of Biological Chemistry

L. Liang and K. L. Lim and K. T. Seow and C. H. Ng and C. J. Pallen

DOI: 10.1074/jbc.m004843200

07 / 2000

Isolation of a novel protein tyrosine phosphatase inhibitor, 2-methyl-fervenulone, and its precursors from Streptomyces

Journal of Natural Products

Wang, H. and Kah Leong Lim, and Su Ling Yeo, and Xu, X. and Mui Mui Sim, and Ting, A.E. and Wang, Y. and Yee, S. and Tan, Y.H. and Pallen, C.J.

DOI: 10.1021/np000293+

Calmodulin binds to and inhibits the activity of the membrane distal catalytic domain of receptor protein-tyrosine phosphatase a

Journal of Biological Chemistry

Liang, L. and Lim, K.L. and Seow, K.T. and Ng, C.H. and Pallen, C.J.

Prenylation-dependent association of protein-tyrosine phosphatases PRL- 1, -2, and -3 with the plasma membrane and the early endosome

Journal of Biological Chemistry

Zeng, Q. and Si, X. and Horstmann, H. and Xu, Y. and Hong, W. and Pallen, C.J.

DOI: 10.1074/jbc.M000453200

Targeted disruption of the tyrosine phosphatase PTPa leads to constitutive downregulation of the kinases Src and Fyn

Current Biology

Sathivel Ponniah and Dennis Z.M. Wang and Kah Leong Lim and Catherine J. Pallen

DOI: 10.1016/s0960-9822(99)80238-3

05 / 1999

Catalytic activation of the membrane distal domain of protein tyrosine phosphatase e, but not CD45, by two point mutations

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Lim, K.L. and Ng, C.H. and Pallen, C.J.

DOI: 10.1016/S0167-4838(99)00189-2

Protein tyrosine phosphatase a (PTPa) and contactin form a novel neuronal receptor complex linked to the intracellular tyrosine kinase fyn

Journal of Cell Biology

Zeng, L. and D'Alessandri, L. and Kalousek, M.B. and Vaughan, L. and Pallen, C.J.

DOI: 10.1083/jcb.147.4.707

Solid-phase synthesis of potential protein tyrosine phosphatase inhibitors via the Ugi four-component condensation

Bioorganic & Medicinal Chemistry Letters

Zhengong Li and Su Ling Yeo and Catherine J. Pallen and A. Ganesan

DOI: 10.1016/s0960-894x(98)00408-9

09 / 1998

Antibodies to the Protein Tyrosine Phosphatases IAR and IA-2 are Associated with Progression to Insulin-Dependent Diabetes (IDDM) in First-Degree Relatives At-Risk for IDDM

Autoimmunity

Robert S. Schmidli and Peter G. Colman and Lin Cui and Wei-Ping Yu and Kim Kewming and Connie Jankulovski and Leonard C. Harrison and Catherine J. Pallen and Henry J. Deaizpurua

DOI: 10.3109/08916939808993841

01 / 1998

Physical and functional interactions between receptor-like protein- tyrosine phosphatase a and p59(fyn)

Journal of Biological Chemistry

Bhandari, V. and Lim, K.L. and Pallen, C.J.

DOI: 10.1074/jbc.273.15.8691

Insulin secretagogues activate the secretory granule receptor-like protein-tyrosine phosphatase IAR

Journal of Biological Chemistry

Cui, L. and Yu, W.-P. and Pallen, C.J.

DOI: 10.1074/jbc.273.52.34784

Interconversion of the kinetic identities of the tandem catalytic domains of receptor-like protein-tyrosine phosphatase PTPa by two point mutations is synergistic and substrate-dependent

Journal of Biological Chemistry

Lim, K.L. and Kolatkar, P.R. and Ng, K.P. and Ng, C.H. and Pallen, C.J.

DOI: 10.1074/jbc.273.44.28986

Localization of the genes encoding the type I diabetes autoantigens, protein-tyrosine phosphatases IA2 and IAR

Mammalian Genome

Morahan, G. and Huang, D. and Yu, W.-P. and Cui, L. and DeAizpurua, H. and Pallen, C.J.

DOI: 10.1007/s003359900824

Kinetic analysis of two closely related receptor-like protein-tyrosine- phosphatases, PTPa and PTPe

European Journal of Biochemistry

Lim, K.L. and Lai, D.S.Y. and Kalousek, M.B. and Wang, Y. and Pallen, C.J.

Cloning and characterization of islet cell antigen-related protein- tyrosine phosphatase (PTP), a novel receptor-like PTP and autoantigen in insulin-dependent diabetes

Journal of Biological Chemistry

Cui, L. and Yu, W.-P. and DeAizpurua, H.J. and Schmidli, R.S. and Pallen, C.J.

DOI: 10.1074/jbc.271.40.24817

Novel alternative splicing predicts a secreted extracellular isoform of the human receptor-like protein tyrosine phosphatase LAR

Gene

Tabiti, K. and Cui, L. and Chhatwal, V.J.S. and Moochhala, S. and Ngoi, S.S. and Pallen, C.J.

DOI: 10.1016/0378-1119(96)00113-8

Increased mRNA expression of the receptor-like protein tyrosine phosphatase a in late stage colon carcinomas

Cancer Letters

Karim Tabiti and Duncan R. Smith and Hak-Su Goh and Catherine J. Pallen

DOI: 10.1016/0304-3835(95)03816-f

07 / 1995

Expression of receptor-like protein tyrosine phosphatase a in rat embryo fibroblasts activates mitogen-activated protein kinase and c-Jun

Journal of Biological Chemistry

Zheng, X.M. and Pallen, C.J.

The receptor-like protein tyrosine phosphatase a: a role in cell proliferation and oncogenesis

Seminars in Cell Biology

Catherine J. Pallen

DOI: 10.1006/scel.1993.1048

Pituitary-specific transcriptional initiation sites of the rat carboxypeptidase-H gene and the influence of thyroid hormone status.

Molecular Endocrinology

D R Smith and C J Pallen and D Murphy and L Lim

DOI: 10.1210/mend.6.5.1603081

05 / 1992

Pituitary-specific transcriptional initiation sites of the rat carboxypeptidase-H gene and the influence of thyroid hormone status

Molecular Endocrinology

Smith, D.R. and Pallen, C.J. and Murphy, D. and Lim, L.

Protein phosphatases in cell signalling

Current Opinion in Cell Biology

C PALLEN and Y TAN and G GUY

DOI: 10.1016/0955-0674(92)90132-v

Expression and characterization of wild type, truncated, and mutant forms of the intracellular region of the receptor-like protein tyrosine phosphatase HPTP

Journal of Biological Chemistry

Wang, Y. and Pallen, C.J.

Cell transformation and activation of pp60c-src by overexpression of a protein tyrosine phosphatase

Nature

Zheng, X.M. and Wang, Y. and Pallen, C.J.

Elevation of membrane tyrosine phosphatase activity in density-dependent growth-arrested fibroblasts.

Proceedings of the National Academy of Sciences

C. J. Pallen and P. H. Tong

DOI: 10.1073/pnas.88.16.6996

08 / 1991

Purification and characterization of a higher-molecular-mass form of protein phosphotyrosine phosphatase (PTP 1B) from placental membranes

Biochem. J.

C J Pallen and D S Y Lai and H P Chia and I Boulet and P H Tong

DOI: 10.1042/bj2760315

06 / 1991

The receptor-like protein tyrosine phosphatase HPTPa has two active catalytic domains with distinct substrate specificities

EMBO Journal

Wang, V. and Pallen, C.J.

Elevation of membrane tyrosine phosphatase activity in density-dependent growth-arrested fibroblasts

Proceedings of the National Academy of Sciences of the United States of America

Pallen, C.J. and Tong, P.H.

Calcium-dependent and phosphorylation-stimulated proteolysis of lipocortin I by an endogenous A431 cell membrane protease

Journal of Biological Chemistry

Chuah, S.Y. and Pallen, C.J.

Purification and Characterization of Placental Membrane Phosphotyrosine Phosphatases

Cold Spring Harbor Symposia on Quantitative Biology

C.J. Pallen and L. Sahlin and G. Panayotou and M.D. Waterfield

DOI: 10.1101/sqb.1988.053.01.052

01 / 1988

A putative role for calmodulin in corpus cardiacum stimulated trehalose synthesis in fat body of the american cockroach (Periplaneta americana)

Insect Biochemistry

C.J. Pallen and J.E. Steele

DOI: 10.1016/0020-1790(88)90009-1

01 / 1988

Conversion of a phosphoseryl/threonyl phosphatase into a phosphotyrosyl phosphatase

Biochemical Journal

Goris, J. and Pallen, C.J. and Parker, P.J. and Hermann, J. and Waterfield, M.D. and Merlevede, W.

Purification of a Phosphotyrosine Phesphatase That Dephosphorylates the Epidermal Growth Factor Receptor Autophosphorylation Sites

Ann NY Acad Sci

C. J. PALLEN and G. N. PANAYOTOU and L. SAHLIN and M. D. WATERFIELD

DOI: 10.1111/j.1749-6632.1988.tb22356.x

Purification of a phosphotyrosine phosphatase that dephosphorylates the epidermal growth factor receptor autophosphorylation sites

Annals of the New York Academy of Sciences

Pallen, C.J. and Panayotou, G.N. and Sahlin, L. and Waterfield, M.D.

Characterization of the phosphotyrosyl protein phosphatase activity of calmodulin-dependent protein phosphatase

Journal of Biological Chemistry

Chan, C.P. and Gallis, B. and Blumenthal, D.K. and Pallen, C.J. and Wang, J.H. and Krebs, E.G.

Stoichiometry and dynamic interaction of metal ion activators with calcineurin phosphatase

Journal of Biological Chemistry

Pallen, C.J. and Wang, J.H.

Survey of calcineurin activity towards nonprotein compounds and identification of phosphoenol pyruvate as a substrate

Biochemical and Biophysical Research Communications

Catherine J. Pallen and Mark L. Brown and Hideki Matsui and Katherine J. Mitchell and Jerry H. Wang

DOI: 10.1016/0006-291x(85)90226-8

09 / 1985

Modulation of cAMP effects by Ca2+/calmodulin

Bioessays

Catherine J. Pallen and Rajendra K. Sharma and Jerry H. Wang

DOI: 10.1002/bies.950020306

03 / 1985

Use of fluorinated tyrosine phosphates to probe the substrate specificity of the low molecular weight phosphatase activity of calcineurin

Journal of Biological Chemistry

Martin, B. and Pallen, C.J. and Wang, J.H. and Graves, D.J.

A multifunctional calmodulin-stimulated phosphatase

Archives of Biochemistry and Biophysics

Pallen, C.J. and Wang, J.H.

DOI: 10.1016/0003-9861(85)90279-6

Demonstration of different metal ion-induced calcineurin conformations using a monoclonal antibody

Journal of Biological Chemistry

Matsui, H. and Pallen, C.J. and Adachi, A.-M. and Wang, J.H. and Lam, P.H.

The calmodulin regulatory system.

Current topics in cellular regulation

Wang, J.H. and Pallen, C.J. and Sharma, R.K. and Adachi, A.M. and Adachi, K.

Calcineurin-mediated dephosphorylation of the human placental membrane receptor for epidermal growth factor urogastrone

Biochemistry

Pallen, C.J. and Valentine, K.A. and Wang, J.H. and Hollenberg, M.D.

Calcineurin-phosphatase: Ni2+-binding properties

Federation Proceedings

Pallen, C.J. and Wang, J.H.

A survey of calcineurin activity toward non-protein substrate

Federation Proceedings

Wang, J.H. and Pallen, C.J. and Brown, M.L. and Mitchell, K.J.

Calcineurin can dephosphorylate the epidermal growth factor receptor of human placental membrane

Federation Proceedings

Pallen, C.J. and Valentine, K.A. and Wang, J.H. and Hollenberg, M.D.

Regulation of calcineurin by metal ions. Mechanism of activation by Ni2+ and an enhanced response to Ca2+/calmodulin

Journal of Biological Chemistry

Pallen, C.J. and Wang, J.H.

Calmodulin-stimulated dephosphorylation of p-nitrophenyl phosphate and free phosphotyrosine by calcineurin

Journal of Biological Chemistry

Pallen, C.J. and Wang, J.W.

Current Project

The lab studies the molecular, cell, and whole animal biology of selected PTPs, in particular the receptor PTPa and the prenylated PRL-PTPs. Characterizing their substrates, pathways of action, regulation, and localization will shed light on their specific cellular and physiological roles, reveal linkages with human pathophysiologies, and facilitate the development of PTP-based disease therapies. We are particularly interested in the roles of PTPs in pediatric malignancies.

We have identified the transmembrane PTPa as a potential oncogene and as a physiological activator of the proto-oncogene src family kinases. We are elucidating the signal transduction and biological functions of PTPa using PTPa knockout mice and cells that we have generated. One line of study involves the role of PTPa in integrin signalling. Integrins are essential for several cell processes, including growth, migration, and survival. They are thus positioned to determine, and have indeed been implicated in, multiple aspects of cancer cell biology such as invasion and metastasis. In the absence of PTPa, integrin stimulated cell migration and spreading are defective due to impaired early and integrin-proximal signalling events. The molecular basis of these defects is under investigation. Other studies are pursuing the linkage of additional novel defects observed in the PTPa knockout mice to altered cell signalling pathways and function in neurobiology (myelination, NMDA receptor function) and immunology (T cell activation, mast cell function).

The intracellular PRL-PTPs (PRL-1, -2, -3) are closely related prenylated PTPs of unknown function. PRL-3 expression has been recently found to be upregulated in several metastatic cancers. Farnesyltransferase inhibitors (FTI) are anti-tumor agents that were originally designed to block the function of the ras oncogene product. However, in many tumors, these inhibitors act on unidentified non-ras targets. We have shown that the PRLs are potential targets of these inhibitors. FTI induces the relocalization of the PRL-PTPs from the plasma membrane and early endosome to the nucleus, with the likely consequence of altering substrate availability and/or PRL-PTP functions. Our studies are directed to identifying plasma membrane/early endosome-specific versus nuclear-specific PRL-PTP substrates and interacting proteins. This will pinpoint alternate PRL-PTP functions and signalling pathways that may be relevant to tumorigenesis or tumor progression. Additionally, we are examining PRL-PTP expression in a range of primary and metastatic tumors to ascertain whether altered PRL-PTP levels correlate with malignancy status.

Grants

Cancer Research Society Grant

Honours & Awards

National Science Award, Singapore - 1995

MacMillan Distinguished Lecturer, Rutgers University - 2000

Outstanding University Researcher Award 1999/2000, National University of Singapore - 2001

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BC Children's Hospital Research Institute operates on the ancestral and unceded territory of the Coast Salish peoples — xʷməθkʷəy̓əm (Musqueam), Sḵwx̱wú7mesh (Squamish), and Səl̓ílwətaʔ/Selilwitulh (Tsleil-Waututh) Nations. Further, this acknowledgement, gratitude, and respect extends to all of the First Nations communities on whose territories the Research Institute builds relationships and operates in British Columbia.

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