Organization of the human PTK7 gene encoding a receptor protein tyrosine kinase-like molecule and alternative splicing of its mRNA

Jung, Jaewon; Ji, Ae Ri; Lee, Jonghyeob; Kim, Ung Jin; Lee, Seung Taek

doi:10.1016/s0167-4781(02)00536-5

Cited by 34 publications

(37 citation statements)

References 39 publications

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“…Clade 7 proteins showed homology to the meiosis regulatory proteins (Kaur et al, 2006). RBPs in Clade 8 showed homology to proteins involved in mRNA splicing and also to those that act as transcriptional coactivators (Jung et al, 2002). Based on these similarities to well characterized eukaryotic RBPs, it is obvious that plant RBPs with triple RRMs have diverse cellular functions.This analysis provides a good starting point to examine the precise functional roles of each of these proteins in plants.…”

Section: Discussionmentioning

confidence: 99%

Phylogenetic and Expression Analysis of RNA-binding Proteins with Triple RNA Recognition Motifs in Plants

Peal¹,

Jambunathan²,

Mahalingam³

2011

Molecules and Cells

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The superfamily of RNA binding proteins (RBPs) is vastly expanded in plants compared to other eukaryotes. A subfamily of RBPs that contain three RNA recognition motifs (RRMs) from the Arabidopsis (24), rice (19) and poplar (37) genomes was analyzed in this study. Phylogenetic analysis with full-length protein sequences of 80 RBPs identified nine clades. The largest clade, comprising 23 members, showed high homology to human RBPs involved in oxidative signaling. Digital northern analysis revealed that Arabidopsis RBPs are transcriptionally responsive to biotic, abiotic and hormonal treatments. Northern blot analysis of eight Arabidopsis RBPs belonging to the tobacco RBP45/47 family showed that these genes respond to ozone stress. AtRBP45b, which shows closest homology to the yeast oxidative stress regulatory protein, CSX1, was expressed in multiple tissues. Two novel splice variant forms of AtRBP45b were identified by 3'RACE analysis. Based on RT-PCR, splice variant AtRBP45b-SV1 was observed only in response to mechanical wounding caused by pathogen or chemical infiltrations and was not detectable in response to salt or temperature stress. Electrophoretic mobility shift assay demonstrated that recombinant full-length and splice variant forms of AtRBP45b bound synthetic RNA. Identifying in vivo RNA targets of AtRBP45b will aid in determining the precise functional role of these proteins during oxidative signaling.

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Section: Discussionmentioning

confidence: 99%

Phylogenetic and Expression Analysis of RNA-binding Proteins with Triple RNA Recognition Motifs in Plants

Peal¹,

Jambunathan²,

Mahalingam³

2011

Molecules and Cells

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“…Ptk7-deficient mouse embryos show all signs of typical PCP defects, such as severe neural tube and abdomen closure defects with secondary development abnormalities (21). PTK7 is a type I protein composed of seven Ig loops in its extracellular region, a transmembrane domain, and an intracellular region with a tyrosine kinase domain (17,18,22,23). Although PTK7 is catalytically inactive, the cytoplasmic domain containing the tyrosine kinase domain is mandatory for receptor function in vitro and in vivo (24)(25)(26)(27).…”

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confidence: 99%

Ptk7-Deficient Mice Have Decreased Hematopoietic Stem Cell Pools as a Result of Deregulated Proliferation and Migration

Lhoumeau

Arcangeli

Grandis

et al. 2016

The Journal of Immunology

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International audienceHematopoietic stem cells (HSCs) located in adult bone marrow or fetal liver in mammals produce all cells from the blood system. Atthe top of the hierarchy are long-term HSCs endowed with lifelong self-renewal and differentiation properties. These features arecontrolled through key microenvironmental cues and regulatory pathways, such as Wnt signaling.We showed previously that PTK7,a tyrosine kinase receptor involved in planar cell polarity, plays a role in epithelial Wnt signaling; however, its function in hematopoiesishas remained unexplored. In this article, we show that PTK7 is expressed by hematopoietic stem and progenitor cells, withthe highest level of protein expression found on HSCs. Taking advantage of a Ptk7-deficient mouse strain, we demonstrate that loss ofPtk7 leads to a diminished pool of HSCs but does not affect in vitro or in vivo hematopoietic cell differentiation. This is correlatedwith increased quiescence and reduced homing abilities of Ptk7-deficient hematopoietic stem and progenitor cells, unraveling noveland unexpected functions for planar cell polarity pathways in HSC fate

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“…Ubiquitously expressed PTK7 (also called colon carcinoma kinase-4 (CCK-4)) is a Wnt coreceptor and a regulator of PCP in vertebrates (7)(8)(9)(10)(11)(12)(13). Membrane PTK7 includes seven extracellular Ig domains, a transmembrane region, and a catalytically inert cytoplasmic tyrosine kinase (PTK) domain (8,9,11,14).…”

mentioning

confidence: 99%

“…Membrane PTK7 includes seven extracellular Ig domains, a transmembrane region, and a catalytically inert cytoplasmic tyrosine kinase (PTK) domain (8,9,11,14). PTK7 is evolutionary conserved in humans and mice and also chicken klingon (KLG), Drosophila (Dtrk/Off-track), and hydra (Lemon) (7).…”

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confidence: 99%

Potential Relation of Aberrant Proteolysis of Human Protein Tyrosine Kinase 7 (PTK7) chuzhoi by Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) to Congenital Defects

Golubkov

Aleshin

Strongin

2011

Journal of Biological Chemistry

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Membrane PTK7 pseudo-kinase plays an essential role in planar cell polarity and the non-canonical Wnt pathway in vertebrates. Recently, a new N-ethyl-N-nitrosourea-induced mutant named chuzhoi (chz) was isolated in mice. chz embryos have severe birth defects, including a defective neural tube, defective heart and lung development, and a shortened anterior-posterior body axis. The chz mutation was mapped to the Ala-Asn-Pro tripeptide insertion into the junction region between the fifth and the sixth Ig-like domains of PTK7. Unexpectedly, chz reduced membrane localization of the PTK7 protein. We hypothesized and then proved that the chz mutation caused an insertion of an additional membrane type 1 matrix metalloproteinase cleavage site in PTK7 and that the resulting aberrant proteolysis of chz affected the migratory parameters of the cells. It is likely that aberrations in the membrane type 1 matrix metalloproteinase/PTK7 axis are detrimental to cell movements that shape the body plan and that chz represents a novel model system for increasing our understanding of the role of proteolysis in developmental pathologies, including congenital defects.About three of every 100 babies born in the United States have congenital abnormalities. Congenital abnormalities are ranked 34th of the top 50 causes of total death in the United States. Debilitating cardiovascular and nervous system defects jointly represent 40% of birth defects. The death toll of congenital abnormalities (0.58%) roughly equals that of stomach, skin, or oral cancers. Mechanistic research into birth defects is required to more efficiently contribute to prevention and correction of these disorders.The canonical, ␤-catenin-dependent and non-canonical, ␤-catenin-independent Wnt signaling pathways are conserved in eukaryotes and are critical for the diverse events in embryonic development and disease. The non-canonical Wnt/planar cell polarity (PCP) 2 signaling controls cell organization within the tissue plane (1, 2). The Wnt/PCP signaling affects the actin cytoskeleton via RhoA GTPase activation through dishevelled associated activator of morphogenesis 1 (DAAM1) and dishevelled activator of morphogenesis 2 (DAAM2). The first PCP signaling events occur at a gastrulation stage of embryogenesis. These events regulate the polarized directed cell movement to accomplish convergent extension for the anterior-posterior body axis elongation, neural tube closure, and craniofacial morphogenesis (3-6). Convergent extension failure results in a shortened anterior-posterior body axis and widened lateral axis (convergent extension phenotype), a defective neural system, and craniofacial abnormalities.Ubiquitously expressed PTK7 (also called colon carcinoma kinase-4 (CCK-4)) is a Wnt coreceptor and a regulator of PCP in vertebrates (7-13). Membrane PTK7 includes seven extracellular Ig domains, a transmembrane region, and a catalytically inert cytoplasmic tyrosine kinase (PTK) domain (8,9,11,14). PTK7 is evolutionary conserved in humans and mice and also chicken klingon (KLG...

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Organization of the human PTK7 gene encoding a receptor protein tyrosine kinase-like molecule and alternative splicing of its mRNA

Cited by 34 publications

References 39 publications

Phylogenetic and Expression Analysis of RNA-binding Proteins with Triple RNA Recognition Motifs in Plants

Phylogenetic and Expression Analysis of RNA-binding Proteins with Triple RNA Recognition Motifs in Plants

Ptk7-Deficient Mice Have Decreased Hematopoietic Stem Cell Pools as a Result of Deregulated Proliferation and Migration

Potential Relation of Aberrant Proteolysis of Human Protein Tyrosine Kinase 7 (PTK7) chuzhoi by Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) to Congenital Defects

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