Characterization of the Carboxyl-terminal Domain of the Rat Glucose-dependent Insulinotropic Polypeptide (GIP) Receptor

Thrombopoietin (TPO), the ligand for c-mpl, is a novel cytokine comprising an amino terminal domain with homology to erythropoietin and a glycosylated carboxyl terminal domain that does not bear overall homology to other known proteins. We report the cloning of cDNAs encoding the porcine and murine TPO and the characterization of the human TPO gene. The cDNA for an additional splice form (TPO-2) with a four-amino-acid deletion within the erythropoietin-like domain has been isolated and is conserved between humans, pigs, and mice. Species comparison of TPO shows that the amino terminal erythropoietin-like domain is highly conserved, while the carboxyl terminal domain is less conserved. Recombinant murine TPO and human TPO are each able to activate both the murine and human c-mpl receptors, indicating an absence of strict species specificity. Human TPO is encoded by a single gene consisting of six exons and located on chromosome 3q271–28.

Download Full-text

Characterization of the Connexin45 Carboxyl-Terminal Domain Structure and Interactions with Molecular Partners

Biophysical Journal ◽

10.1016/j.bpj.2014.03.045 ◽

2014 ◽

Vol 106 (10) ◽

pp. 2184-2195 ◽

Cited By ~ 12

Author(s):

Jennifer L. Kopanic ◽

Mona H. Al-mugotir ◽

Fabien Kieken ◽

Sydney Zach ◽

Andrew J. Trease ◽

...

Keyword(s):

Domain Structure ◽

Terminal Domain ◽

Carboxyl Terminal Domain ◽

Carboxyl Terminal

Download Full-text

Characterization of Mutants Affecting the KRK Sequence in the Carboxyl-terminal Domain oflacRepressor

Journal of Biological Chemistry ◽

10.1074/jbc.270.18.10640 ◽

1995 ◽

Vol 270 (18) ◽

pp. 10640-10649 ◽

Cited By ~ 9

Author(s):

Likun Li ◽

Kathleen Shive Matthews

Keyword(s):

Terminal Domain ◽

Carboxyl Terminal Domain ◽

Carboxyl Terminal

Download Full-text

Functional Characterization of a Nup159p-containing Nuclear Pore Subcomplex

Molecular Biology of the Cell ◽

10.1091/mbc.9.12.3475 ◽

1998 ◽

Vol 9 (12) ◽

pp. 3475-3492 ◽

Cited By ~ 67

Author(s):

Naı̈ma Belgareh ◽

Christine Snay-Hodge ◽

Fabien Pasteau ◽

Suzanne Dagher ◽

Charles N. Cole ◽

...

Keyword(s):

Protein Import ◽

Functional Characterization ◽

Nuclear Pore ◽

Terminal Domain ◽

Carboxyl Terminal Domain ◽

Cytoplasmic Face ◽

Rna Export ◽

Carboxyl Terminal

Nup159p/Rat7p is an essential FG repeat–containing nucleoporin localized at the cytoplasmic face of the nuclear pore complex (NPC) and involved in poly(A)+RNA export and NPC distribution. A detailed structural–functional analysis of this nucleoporin previously demonstrated that Nup159p is anchored within the NPC through its essential carboxyl-terminal domain. In this study, we demonstrate that Nup159p specifically interacts through this domain with both Nsp1p and Nup82p. Further analysis of the interactions within the Nup159p/Nsp1p/Nup82p subcomplex using the nup82Δ108mutant strain revealed that a deletion within the carboxyl-terminal domain of Nup82p prevents its interaction with Nsp1p but does not affect the interaction between Nup159p and Nsp1p. Moreover, immunofluorescence analysis demonstrated that Nup159p is delocalized from the NPC in nup82Δ108 cells grown at 37°C, a temperature at which the Nup82Δ108p mutant protein becomes degraded. This suggests that Nup82p may act as a docking site for a core complex composed of the repeat-containing nucleoporins Nup159p and Nsp1p. In vivo transport assays further revealed that nup82Δ108and nup159-1/rat7-1 mutant strains have little if any defect in nuclear protein import and protein export. Together our data suggest that the poly(A)+RNA export defect previously observed in nup82 mutant cells might be due to the loss from the NPCs of the repeat-containing nucleoporin Nup159p.

Download Full-text