A Novel GTPase-activating Protein for Rho Interacts with a PDZ Domain of the Protein-tyrosine Phosphatase PTPL1

Saras, Jan; Franzén, Petra; Aspenström, Pontus; Hellman, Ulf; Góñez, L. Jorge; Heldin, Carl‐Henrik

doi:10.1074/jbc.272.39.24333

Cited by 119 publications

(116 citation statements)

References 38 publications

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“…PARG1 codes for PTPL1-associated RhoGAP1, a GTPase-activating protein (GAP) that exhibits in vitro GAP activity towards the Rho-and Ras-family members Rho 48 and Rap2, 49 thus promoting a switch from the active to the inactive form 50 and that may, therefore, act as a suppressor of Rho-and Ras-mediated cellular transformation. 50 Recently, Ghobrial and co-workers reported on the overexpression of the guanine nucleotide exchange factor RCC1 (regulator of chromosome condensation 1) and the RhoA-dependent kinase CRIK (citron Rho-interacting kinase) in MCL, suggesting that alterations of the Rho-Ras-network may be involved in the pathogenesis of MCL.…”

Section: Discussionmentioning

confidence: 99%

Promoter methylation of PARG1, a novel candidate tumor suppressor gene in mantle cell lymphomas

Ripperger¹,

Neuhoff²,

Kamphues³

et al. 2007

Haematologica

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Section: Discussionmentioning

confidence: 99%

Promoter methylation of PARG1, a novel candidate tumor suppressor gene in mantle cell lymphomas

Ripperger¹,

Neuhoff²,

Kamphues³

et al. 2007

Haematologica

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“…The tyrosine phosphatase LAR has been localized to focal adhesions (99), and cells from mice deficient in LAR or the closely related PTP demonstrate impairment of cell migration (100 -102). LAR and the tyrosine phosphatase PTPL1 appear to regulate cell motility through interactions with the Rho and Rac G proteins (103,104). SHP-2 and PTEN have been shown to negatively regulate focal adhesion signaling by mediating FAK dephosphorylation (105)(106)(107)(108), while PTP-PEST has been shown to mediate p130Cas dephosphorylation (109,110) and associate with paxillin (111).…”

Section: Discussionmentioning

confidence: 99%

Deficiency of Src Homology 2-Containing Phosphatase 1 Results in Abnormalities in Murine Neutrophil Function: Studies inMotheatenMice

Kruger

Butler

Cherapanov

et al. 2000

The Journal of Immunology

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Neutrophils, an essential component of the innate immune system, are regulated in part by signaling pathways involving protein tyrosine phosphorylation. While protein tyrosine kinase functions in regulating neutrophil behavior have been extensively investigated, little is known about the role for specific protein tyrosine phosphatases (PTP) in modulating neutrophil signaling cascades. A key role for Src homology 2 domain-containing phosphatase 1 (SHP-1), a PTP, in neutrophil physiology is, however, implied by the overexpansion and inappropriate activation of granulocyte populations in SHP-1-deficient motheaten (me/me) and motheaten viable (mev/mev) mice. To directly investigate the importance of SHP-1 to phagocytic cell function, bone marrow neutrophils were isolated from both me/me and mev/mev mice and examined with respect to their responses to various stimuli. The results of these studies revealed that both quiescent and activated neutrophils from motheaten mice manifested enhanced tyrosine phosphorylation of cellular proteins in the 60- to 80-kDa range relative to that detected in wild-type congenic control neutrophils. Motheaten neutrophils also demonstrated increased oxidant production, surface expression of CD18, and adhesion to protein-coated plastic. Chemotaxis, however, was severely diminished in the SHP-deficient neutrophils relative to control neutrophils, which was possibly attributable to a combination of defective deadhesion and altered actin assembly. Taken together, these results indicate a significant role for SHP-1 in modulating the tyrosine phosphorylation-dependent signaling pathways that regulate neutrophil microbicidal functions.

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“…PTP-BL is a nontransmembrane protein tyrosine phosphatase implicated in the modulation of the cytoskeleton. Binding of PTP-BL to proteins such as RhoGAP protein, RIL or the zyxin related protein ZRP-1 suggest an involvement in the dynamic changes of the actin cytoskeleton (Saras et al, 1997;Cuppen et al, 1998;Murthy et al, 1999). However, a de®ned function of this protein tyrosine phosphatase is still missing.…”

Section: Introductionmentioning

confidence: 99%

The Adenomatous Polyposis Coli-protein (APC) interacts with the protein tyrosine phosphatase PTP-BL via an alternatively spliced PDZ domain

Erdmann

Kuhlmann²,

Leßmann

et al. 2000

Oncogene

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Mutations of the tumor suppressor protein APC (Adenomatous Polyposis Coli) are linked to familiar and sporadic human colon cancer. Here we describe a novel interaction between the APC protein and the protein tyrosine phosphatase PTP-BL carrying ®ve PDZ protein ± protein interaction domains. Exclusively, the second PDZ domain (PDZ2) of PTP-BL is binding to the extreme C-terminus of the APC protein, as determined by yeast two-hybrid studies. Using surface plasmon resonance analysis we established a dissociation constant (K D ) of 8.1610 79 M. We ®nd that a naturally occurring splice insertion of ®ve amino acids (PDZ2b) abolishes its binding a nity to the APC protein. The in vivo interaction between PTP-BL and the APC protein was shown by coprecipitation experiments in transfected COS cells. Furthermore, in cultured epithelial Madine Carnine Kidney cells the subcellular colocalization was demonstrated for the nucleus and also for the tips of cellular extensions. The interaction of the APC protein with a protein tyrosine phosphatase may indirectly modulate the steady state levels of tyrosine phosphorylations of associated proteins, such as b-catenin playing a major role in the regulation of cell division, migration and cell adhesion. Oncogene (2000) 19, 3894 ± 3901.

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A Novel GTPase-activating Protein for Rho Interacts with a PDZ Domain of the Protein-tyrosine Phosphatase PTPL1

Cited by 119 publications

References 38 publications

Promoter methylation of PARG1, a novel candidate tumor suppressor gene in mantle cell lymphomas

Promoter methylation of PARG1, a novel candidate tumor suppressor gene in mantle cell lymphomas

Deficiency of Src Homology 2-Containing Phosphatase 1 Results in Abnormalities in Murine Neutrophil Function: Studies inMotheatenMice

The Adenomatous Polyposis Coli-protein (APC) interacts with the protein tyrosine phosphatase PTP-BL via an alternatively spliced PDZ domain

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