PMID- 10652311
OWN - NLM
STAT- MEDLINE
DCOM- 20000302
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 275
IP  - 5
DP  - 2000 Feb 4
TI  - Molecular and functional characterization of protein 4.1B, a novel member of the 
      protein 4.1 family with high level, focal expression in brain.
PG  - 3247-55
AB  - 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.
FAU - Parra, M
AU  - Parra M
AD  - Life Sciences Division, Lawrence Berkeley National Laboratory, University of
      California, Berkeley, California 94720, USA.
FAU - Gascard, P
AU  - Gascard P
FAU - Walensky, L D
AU  - Walensky LD
FAU - Gimm, J A
AU  - Gimm JA
FAU - Blackshaw, S
AU  - Blackshaw S
FAU - Chan, N
AU  - Chan N
FAU - Takakuwa, Y
AU  - Takakuwa Y
FAU - Berger, T
AU  - Berger T
FAU - Lee, G
AU  - Lee G
FAU - Chasis, J A
AU  - Chasis JA
FAU - Snyder, S H
AU  - Snyder SH
FAU - Mohandas, N
AU  - Mohandas N
FAU - Conboy, J G
AU  - Conboy JG
LA  - eng
SI  - GENBANK/AF152247
GR  - P01 DK032094/DK/NIDDK NIH HHS/United States
GR  - DK32094/DK/NIDDK NIH HHS/United States
GR  - HL45182/HL/NHLBI NIH HHS/United States
GR  - MH18501/MH/NIMH NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (DNA, Complementary)
RN  - 0 (Membrane Proteins)
RN  - 0 (Neuropeptides)
RN  - 0 (Protein Isoforms)
RN  - 0 (erythrocyte membrane band 4.1 protein)
RN  - 0 (erythrocyte membrane protein band 4.1-like 1)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Brain/cytology/*metabolism
MH  - Cell Differentiation
MH  - *Cytoskeletal Proteins
MH  - DNA, Complementary/analysis/genetics
MH  - Gene Expression
MH  - Membrane Proteins/*biosynthesis/genetics
MH  - Mice
MH  - Molecular Sequence Data
MH  - Neurons/cytology/metabolism
MH  - *Neuropeptides
MH  - Protein Isoforms/biosynthesis/genetics
MH  - Sequence Alignment
EDAT- 2000/02/01 09:00
MHDA- 2000/03/04 09:00
CRDT- 2000/02/01 09:00
PHST- 2000/02/01 09:00 [pubmed]
PHST- 2000/03/04 09:00 [medline]
PHST- 2000/02/01 09:00 [entrez]
AID - 10.1074/jbc.275.5.3247 [doi]
PST - ppublish
SO  - J Biol Chem. 2000 Feb 4;275(5):3247-55. doi: 10.1074/jbc.275.5.3247.