Molecular cloning of two novel transmembrane ligands for Eph-related kinases (LERKS) that are related to LERK-2.
A search of the nucleic acid database of expressed sequence tags (ESTs) revealed several partial cDNA sequences that could encode proteins homologous to the ligands for Eph-related kinases (LERKs). Oligonucleotides designed from the ESTs were used to probe a human brain cDNA library and obtain overlapping clones that encoded two different novel LERKS (NLERK-1 and NLERK-2). NLERK-1 and NLERK-2 are most closely related to human LERK-2/Elk-ligand and they form a subclass of LERKs that contain a transmembrane domain and a conserved cytoplasmic domain. Full-length NLERK-1 was expressed as a glycosylated membrane protein in COS cells and was not secreted into the medium. Full-length NLERK-2 was similarly expressed in COS cells but both membrane-bound and a truncated, proteolytically-released form were detected. Engineered forms of both NLERK-1 and NLERK-2 lacking transmembrane and cytoplasmic domains were also expressed in COS cells and each was detected in the extracellular medium.
Nicola
N A
NA
Walter and Eliza Hall Institute of Medical Research, Royal Melbourne Hospital, Victoria, Australia.
Viney
E
E
Hilton
D J
DJ
Roberts
B
B
Willson
T
T
D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D019556:COS Cells; D003001:Cloning, Molecular; D017931:DNA Primers; D016208:Databases, Factual; D004591:Electrophoresis, Polyacrylamide Gel; D036382:Ephrin-A1; D036387:Ephrin-B1; D005819:Genetic Markers / Q000235:genetics; D005822:Genetic Vectors / Q000235:genetics; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D011506:Proteins / Q000737:chemistry*; D016415:Sequence Alignment; D017421:Sequence Analysis
D017931:DNA Primers; D036382:Ephrin-A1; D036387:Ephrin-B1; D005819:Genetic Markers; D008565:Membrane Proteins; D011506:Proteins