Molecular cloning and developmental expression of Par-1/MARK homologues XPar-1A and XPar-1B from Xenopuslaevis
نویسندگان
چکیده
Par-1 encodes a serine/threonine kinase that is involved in asymmetric segregation of cell fate determinants in Caenorhabditis elegans and Drosophila embryos. Recent biochemical studies indicate an association of PAR-1 with the Dishevelled protein and suggest a role in so-called canonical Wnt signaling (Nat. Cell Biol. 3 (2001) 628). Here we describe two Xenopus laevis cDNAs, which encode PAR-1 homologues designated XPar-1A and XPar-1B. Structurally, XPar-1A and XPar-1B are closely related to rat MARK proteins and human Par-1A and Par-1Balpha, respectively. XPar-1A and XPar-1B are expressed both maternally and zygotically in an indistinguishable pattern. In the egg and cleavage stage embryos their transcripts are enriched in the animal pole of the embryo. During blastula and gastrula stages, cells in the animal and marginal regions continue to express both genes uniformly. Expression progresses vegetally towards and then through the blastopore lip concomitantly with the movements of epiboly and gastrulation. With the onset of neurulation, XPar-1A and XPar-1B transcripts are restricted to the neurectoderm. At tailbud and tadpole stages they are detected in the head region, including brain, eyes, otic vesicles, cement gland, branchial arches as well as spinal cord and somites. Therefore, this analysis suggests that the Xenopus par-1 homologues XPar-1A and XPar-1B are expressed in frog embryos both maternally and zygotically in a restricted pattern and may play a role in establishing polarity in early embryos as well as in organogenesis during later stages of development.
منابع مشابه
Identification and developmental expression of par-6 gene in Xenopus laevis
The par genes (partitioning defective) are required to establish polarity in the Caenorhabditis elegans embryo. We have identified the Xenopus homologue of C. elegans PAR-6 (XPAR-6). XPAR-6 is a protein of 377 amino acids with one PDZ domain which is involved in mediating protein-protein interactions. It shares 59% and 58% amino acid identity with the mouse and Drosophila PAR-6, respectively, a...
متن کاملContents continued
Novel sites of expression of the bHLH gene NSCL1 in the developing nervous system S103 Expression profiles of the connexin genes, Gjb1 and Gjb3, in the developing mouse cochlea S111 Widespread expression of an extended peptide sequence of GATA-6 during murine embryogenesis and non-equivalence of RNA and protein expression domains S121 F. Bajanca, S. Thorsteinsdóttir (Portugal) Integrin expressi...
متن کاملThe polarity-inducing kinase Par-1 controls Xenopus gastrulation in cooperation with 14-3-3 and aPKC.
Par (partitioning-defective) genes were originally identified in Caenorhabditis elegans as determinants of anterior/posterior polarity. However, neither their function in vertebrate development nor their action mechanism has been fully addressed. Here we show that two members of Par proteins, 14-3-3 (Par-5) and atypical PKC (aPKC), regulate the serine/threonine kinase Par-1 to control Xenopus g...
متن کاملLoss of Par-1a/MARK3/C-TAK1 kinase leads to reduced adiposity, resistance to hepatic steatosis, and defective gluconeogenesis.
Par-1 is an evolutionarily conserved protein kinase required for polarity in worms, flies, frogs, and mammals. The mammalian Par-1 family consists of four members. Knockout studies of mice implicate Par-1b/MARK2/EMK in regulating fertility, immune homeostasis, learning, and memory as well as adiposity, insulin hypersensitivity, and glucose metabolism. Here, we report phenotypes of mice null for...
متن کاملMolecular cloning and recombinant expression of the VP28 (wsv421 gene) from Iranian white spot syndrome virus isolate
White spot syndrome virus (WSSV) is a highly pathogenic and prevalent virus affecting shrimp culture worldwide including Iran. In the present study, a pair of primers was designed according to the sequence of VP 28 gene of WSSV in the GenBank. VP28 gene from an Iranian WSSV isolate (IrVP28) was cloned, sequenced and expressed in Escherichia coli BL21(DE3) strain in order to produce VP28 protein...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Mechanisms of Development
دوره 119 شماره
صفحات -
تاریخ انتشار 2002