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Dissecting the sequence specific functions of alternative N-terminal isoforms of mouse bullous pemphigoid antigen 1.

Abstract：

:Bullous pemphigoid antigen 1 (BPAG1) is a member of the plakin family of proteins that is involved in cross-linking the cytoskeletal elements and attaching them to cell junctions. BPAG1 null mice develop severe degeneration of sensory neurons that was attributed in part due to the absence of a splice variant called BPAG1a that harbors an actin-binding domain at the N-terminus. Additional alternative splicing also results in BPAG1a isoforms with different first exons, leading to three additional types of BPAG1a called isoforms 1, 2 and 3 (or BPAG1a1, BPAG1a2, and BPAG1a3). These unique N-terminal extensions of the BPAG1a isoforms are of variable length. In this study, we characterized these N-terminal isoforms and evaluated the influence of these unique N-terminal sequences to the actin-binding properties. The unique N-terminal region of isoform 1 is very short and was not expected to affect the property of the ABD that followed it. In contrast, transfection studies and mutagenesis analyses signified that the N-terminal sequences of isoform 2 had the ability to bundle actin filaments and the N-terminal region that contained isoform 3 showed cortical localization. Isoforms 1, 2 and 3 also displayed differential tissue expression profiles. Taken together, these data suggested that the unique N-terminal regions of these isoforms have different roles that may be tailored to meet tissue specific functions.

journal_name

Exp Cell Res

journal_title

Experimental cell research

authors

Jefferson JJ,Leung CL,Liem RK

doi

10.1016/j.yexcr.2006.04.025

subject

Has Abstract

pub_date

2006-09-10 00:00:00

pages

2712-25

issue

15

eissn

0014-4827

issn

1090-2422

pii

S0014-4827(06)00169-8

journal_volume

312

pub_type

杂志文章

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