Jc. Dunkelberg et A. Gutierrez-hartmann, LZ-FYVE: A novel developmental stage-specific leucine zipper, FYVE-finger protein, DNA CELL B, 20(7), 2001, pp. 403-412
We describe the molecular cloning and characterization of LZ-FYVE, a novel
embryonic factor that possesses two leucine zipper motifs and a FYVE-finger
domain. A partial clone of LZ-FYVE, encoding a functional leucine zipper d
omain, was initially isolated from a mouse embryo cDNA library by virtue of
its interaction in the yeast two-hybrid system with the transcription fact
or ATF-2. The LZ-FYVE protein demonstrated mouse embryo-specific expression
by Northern blot analysis and was detected as a nuclear protein at very re
stricted periods (12-14 days post-coitus) in specific tissues during embryo
genesis. In particular, LZ-FYVE protein was notable in embryonic lung, cart
ilage, and otic capsule. Structural analysis of the deduced, full-length LZ
-FYVE amino acid sequence revealed two N-terminal leucine zipper domains as
well as a C-terminal FYVE-finger domain. The FYVE-finger domains specifica
lly recognized phosphatidylinositol 3-phosphate and have been previously de
scribed only in cytoplasmic proteins involved in endosomal membrane fusion,
vesicular trafficking, or organelle-specific targeting. While LZ-FYVE may
have endosomal functions in the cytoplasm, because LZ-FYVE is present in th
e nucleus at early stages of embryonic development, it is likely that LZ-FY
VE has a nuclear function.