Characterization of a novel splicing variant of KLHL5 ^*, a member of the kelch protein family

Abstract

The kelch-repeat protein family is a recently found new kind of actin-binding protein. It is characterized by tandemly arranged motifs of about 50 amino acids [7]. Previous study showed that most members of the kelch-repeat family were cytoskeletal proteins implicated in various cellular processes, such as actin cytoskeleton interaction, cytoplasmic sequestration of transcription factors and cell morphology [1]. And some of the family members play important roles in tissue development, such as human ENC-1, NRP/B, etc. Another characteristic of the kelch family is that most members have another conserved BTB domain at the extreme amino terminus. The BTB domain is also found at the N-terminus of 5–10% of zinc-finger transcription factor types and is a conserved protein-protein interaction motif [15]. During the large-scale sequencing analysis of a human fetal brain cDNA library we found a novel kelch-like protein gene 5, KLHL5[11], KLHL5 has high identity with Drosophila kelch protein and many other family members. Here we report a novel splicing variants of KLHL5, named KLHL5b and the expression pattern of KLHL5b in many tissues.