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J Biol Chem, Vol. 275, Issue 5, 3247-3255, February 4, 2000
From the Brain-enriched isoforms of skeletal proteins in
the spectrin and ankyrin gene families have been described. Here we
characterize protein 4.1B, a novel homolog of erythrocyte protein 4.1R
that is encoded by a distinct gene. In situ hybridization
revealed high level, focal expression of 4.1B mRNA in select
neuronal populations within the mouse brain, including Purkinje cells
of the cerebellum, pyramidal cells in hippocampal regions CA1-3,
thalamic nuclei, and olfactory bulb. Expression was also detected in
adrenal gland, kidney, testis, and heart. 4.1B protein exhibits high
homology to the membrane binding, spectrin-actin binding, and
C-terminal domains of 4.1R, including motifs for interaction with NuMA
and FKBP13. cDNA characterization and Western blot analysis
revealed multiple spliceoforms of protein 4.1B, with functionally
relevant heterogeneity in the spectrin-actin and NuMA binding domains. Regulated alternative splicing events led to expression of unique 4.1B
isoforms in brain and muscle; only the latter possessed a functional
spectrin-actin binding domain. By immunofluorescence, 4.1B was
localized specifically at the plasma membrane in regions of cell-cell
contact. Together these results indicate that 4.1B transcription is
selectively regulated among neuronal populations and that alternative
splicing regulates expression of 4.1B isoforms possessing critical
functional domains typical of other protein 4.1 family members.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF152247.
Molecular and Functional Characterization of Protein 4.1B, a
Novel Member of the Protein 4.1 Family with High Level, Focal
Expression in Brain*
§,§,,,
,,,, and
Life Sciences Division, Lawrence Berkeley
National Laboratory, University of California, Berkeley, California
94720, the ¶ Department of Neuroscience, Johns Hopkins University
School of Medicine, Baltimore, Maryland 21205, the Department of
Biochemistry, School of Medicine, Tokyo Women's Medical University,
Tokyo 162, Japan, and the ** Department of Animal Science, University of
California, Davis, California 95616
*
This work was supported by United States Public Health
Service Grants MH18501 (to S. H. S.), HL45182 (to J. G. C.), and
DK32094 (to N. M.) and Research Scientist Grant DA-0074 (to
S. H. S.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Life Sciences
Division, MS 74-174, Lawrence Berkeley National Laboratory, Berkeley, CA 94720. Tel.: 510-486-6973; Fax: 510-486-6746.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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