Full text data of BMF
BMF
[Confidence: low (only semi-automatic identification from reviews)]
Bcl-2-modifying factor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Bcl-2-modifying factor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96LC9
ID BMF_HUMAN Reviewed; 184 AA.
AC Q96LC9; Q2M396; Q6NT30; Q6NT56; Q6P9F6; Q7Z7D4; Q7Z7D5; Q9H7K7;
read moreDT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 86.
DE RecName: Full=Bcl-2-modifying factor;
GN Name=BMF;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=T-cell;
RX PubMed=11546872; DOI=10.1126/science.1062257;
RA Puthalakath H., Villunger A., O'Reilly L.A., Beaumont J.G.,
RA Coultas L., Cheney R.E., Huang D.C.S., Strasser A.;
RT "Bmf: a proapoptotic BH3-only protein regulated by interaction with
RT the myosin V actin motor complex, activated by anoikis.";
RL Science 293:1829-1832(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND TISSUE
RP SPECIFICITY.
RC TISSUE=B-cell;
RX PubMed=14574334; DOI=10.1038/sj.leu.2403183;
RA Morales A.A., Olsson A., Celsing F., Oesterborg A., Jondal M.,
RA Osorio L.M.;
RT "Expression and transcriptional regulation of functionally distinct
RT Bmf isoforms in B-chronic lymphocytic leukemia cells.";
RL Leukemia 18:41-47(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
RX PubMed=11214971; DOI=10.1093/dnares/7.6.357;
RA Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen.";
RL DNA Res. 7:357-366(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May play a role in apoptosis. Isoform 1 seems to be the
CC main initiator.
CC -!- SUBUNIT: Interacts with MCL1, BCL2, BCL2L1/BCL-Xl, BCL2A1 and
CC BCL2L2/BCL-w. Interacts with the myosin V actin motor complex
CC through its binding to DLC2 (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=BMF-I;
CC IsoId=Q96LC9-1; Sequence=Displayed;
CC Name=2; Synonyms=BMF-II;
CC IsoId=Q96LC9-2; Sequence=VSP_012292;
CC Name=3; Synonyms=BMF-III;
CC IsoId=Q96LC9-3; Sequence=VSP_012293, VSP_012294;
CC -!- TISSUE SPECIFICITY: Isoform 1 is mainly expressed in B-lymphoid
CC cells. Isoform 2 and isoform 3 are mainly expressed in B-CLL and
CC normal B-cells.
CC -!- SIMILARITY: Belongs to the Bcl-2 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH60783.1; Type=Erroneous initiation;
CC Sequence=BAB15762.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AY029254; AAK38748.1; -; mRNA.
DR EMBL; AY222040; AAP22965.1; -; mRNA.
DR EMBL; AY222041; AAP22966.1; -; mRNA.
DR EMBL; AK024472; BAB15762.1; ALT_INIT; mRNA.
DR EMBL; BC060783; AAH60783.1; ALT_INIT; mRNA.
DR EMBL; BC069328; AAH69328.1; -; mRNA.
DR EMBL; BC069505; AAH69505.1; -; mRNA.
DR EMBL; BC070043; AAH70043.2; -; mRNA.
DR EMBL; BC104983; AAI04984.1; -; mRNA.
DR EMBL; BC104985; AAI04986.1; -; mRNA.
DR RefSeq; NP_001003940.1; NM_001003940.1.
DR RefSeq; NP_001003942.1; NM_001003942.1.
DR RefSeq; NP_001003943.1; NM_001003943.2.
DR RefSeq; NP_277038.1; NM_033503.3.
DR RefSeq; XP_005254814.1; XM_005254757.1.
DR RefSeq; XP_005254815.1; XM_005254758.1.
DR RefSeq; XP_005254816.1; XM_005254759.1.
DR RefSeq; XP_005254817.1; XM_005254760.1.
DR RefSeq; XP_005254818.1; XM_005254761.1.
DR RefSeq; XP_005254819.1; XM_005254762.1.
DR UniGene; Hs.591104; -.
DR ProteinModelPortal; Q96LC9; -.
DR IntAct; Q96LC9; 4.
DR STRING; 9606.ENSP00000346697; -.
DR PhosphoSite; Q96LC9; -.
DR PRIDE; Q96LC9; -.
DR DNASU; 90427; -.
DR Ensembl; ENST00000220446; ENSP00000220446; ENSG00000104081.
DR Ensembl; ENST00000354670; ENSP00000346697; ENSG00000104081.
DR Ensembl; ENST00000397573; ENSP00000380703; ENSG00000104081.
DR Ensembl; ENST00000431415; ENSP00000396511; ENSG00000104081.
DR Ensembl; ENST00000558774; ENSP00000453913; ENSG00000104081.
DR Ensembl; ENST00000559701; ENSP00000453919; ENSG00000104081.
DR Ensembl; ENST00000561282; ENSP00000453522; ENSG00000104081.
DR Ensembl; ENST00000561360; ENSP00000453892; ENSG00000104081.
DR GeneID; 90427; -.
DR KEGG; hsa:90427; -.
DR UCSC; uc001zkv.4; human.
DR CTD; 90427; -.
DR GeneCards; GC15M040380; -.
DR HGNC; HGNC:24132; BMF.
DR HPA; HPA010120; -.
DR MIM; 606266; gene.
DR neXtProt; NX_Q96LC9; -.
DR PharmGKB; PA134893658; -.
DR eggNOG; NOG40671; -.
DR HOVERGEN; HBG050697; -.
DR InParanoid; Q96LC9; -.
DR KO; K17460; -.
DR OMA; FHRLHMQ; -.
DR OrthoDB; EOG7QRQW6; -.
DR Reactome; REACT_578; Apoptosis.
DR GeneWiki; BMF_(gene); -.
DR GenomeRNAi; 90427; -.
DR NextBio; 76756; -.
DR PRO; PR:Q96LC9; -.
DR ArrayExpress; Q96LC9; -.
DR Bgee; Q96LC9; -.
DR CleanEx; HS_BMF; -.
DR Genevestigator; Q96LC9; -.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0016459; C:myosin complex; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043276; P:anoikis; IDA:MGI.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0032464; P:positive regulation of protein homooligomerization; ISS:BHF-UCL.
DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISS:BHF-UCL.
DR InterPro; IPR028192; BMF.
DR PANTHER; PTHR32014; PTHR32014; 1.
DR Pfam; PF15185; BMF; 1.
DR PROSITE; PS50062; BCL2_FAMILY; FALSE_NEG.
DR PROSITE; PS01259; BH3; FALSE_NEG.
PE 2: Evidence at transcript level;
KW Alternative splicing; Apoptosis; Complete proteome;
KW Reference proteome.
FT CHAIN 1 184 Bcl-2-modifying factor.
FT /FTId=PRO_0000143111.
FT REGION 67 75 Interaction with DLC2 (By similarity).
FT MOTIF 133 147 BH3.
FT VAR_SEQ 98 129 GNAGYRLPLPASFPAVLPIGEQPPEGQWQHQA -> APAEP
FT KSCVVADPPLPAQPCFEWRREQERGRP (in isoform
FT 3).
FT /FTId=VSP_012293.
FT VAR_SEQ 130 184 Missing (in isoform 3).
FT /FTId=VSP_012294.
FT VAR_SEQ 131 151 Missing (in isoform 2).
FT /FTId=VSP_012292.
FT CONFLICT 61 61 R -> Q (in Ref. 4; AAH69328).
FT CONFLICT 80 80 Q -> P (in Ref. 4; AAH69505).
SQ SEQUENCE 184 AA; 20508 MW; 21479B25CC727853 CRC64;
MEPSQCVEEL EDDVFQPEDG EPVTQPGSLL SADLFAQSLL DCPLSRLQLF PLTHCCGPGL
RPTSQEDKAT QTLSPASPSQ GVMLPCGVTE EPQRLFYGNA GYRLPLPASF PAVLPIGEQP
PEGQWQHQAE VQIARKLQCI ADQFHRLHVQ QHQQNQNRVW WQILLFLHNL ALNGEENRNG
AGPR
//
ID BMF_HUMAN Reviewed; 184 AA.
AC Q96LC9; Q2M396; Q6NT30; Q6NT56; Q6P9F6; Q7Z7D4; Q7Z7D5; Q9H7K7;
read moreDT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 86.
DE RecName: Full=Bcl-2-modifying factor;
GN Name=BMF;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=T-cell;
RX PubMed=11546872; DOI=10.1126/science.1062257;
RA Puthalakath H., Villunger A., O'Reilly L.A., Beaumont J.G.,
RA Coultas L., Cheney R.E., Huang D.C.S., Strasser A.;
RT "Bmf: a proapoptotic BH3-only protein regulated by interaction with
RT the myosin V actin motor complex, activated by anoikis.";
RL Science 293:1829-1832(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND TISSUE
RP SPECIFICITY.
RC TISSUE=B-cell;
RX PubMed=14574334; DOI=10.1038/sj.leu.2403183;
RA Morales A.A., Olsson A., Celsing F., Oesterborg A., Jondal M.,
RA Osorio L.M.;
RT "Expression and transcriptional regulation of functionally distinct
RT Bmf isoforms in B-chronic lymphocytic leukemia cells.";
RL Leukemia 18:41-47(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
RX PubMed=11214971; DOI=10.1093/dnares/7.6.357;
RA Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen.";
RL DNA Res. 7:357-366(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May play a role in apoptosis. Isoform 1 seems to be the
CC main initiator.
CC -!- SUBUNIT: Interacts with MCL1, BCL2, BCL2L1/BCL-Xl, BCL2A1 and
CC BCL2L2/BCL-w. Interacts with the myosin V actin motor complex
CC through its binding to DLC2 (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=BMF-I;
CC IsoId=Q96LC9-1; Sequence=Displayed;
CC Name=2; Synonyms=BMF-II;
CC IsoId=Q96LC9-2; Sequence=VSP_012292;
CC Name=3; Synonyms=BMF-III;
CC IsoId=Q96LC9-3; Sequence=VSP_012293, VSP_012294;
CC -!- TISSUE SPECIFICITY: Isoform 1 is mainly expressed in B-lymphoid
CC cells. Isoform 2 and isoform 3 are mainly expressed in B-CLL and
CC normal B-cells.
CC -!- SIMILARITY: Belongs to the Bcl-2 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH60783.1; Type=Erroneous initiation;
CC Sequence=BAB15762.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AY029254; AAK38748.1; -; mRNA.
DR EMBL; AY222040; AAP22965.1; -; mRNA.
DR EMBL; AY222041; AAP22966.1; -; mRNA.
DR EMBL; AK024472; BAB15762.1; ALT_INIT; mRNA.
DR EMBL; BC060783; AAH60783.1; ALT_INIT; mRNA.
DR EMBL; BC069328; AAH69328.1; -; mRNA.
DR EMBL; BC069505; AAH69505.1; -; mRNA.
DR EMBL; BC070043; AAH70043.2; -; mRNA.
DR EMBL; BC104983; AAI04984.1; -; mRNA.
DR EMBL; BC104985; AAI04986.1; -; mRNA.
DR RefSeq; NP_001003940.1; NM_001003940.1.
DR RefSeq; NP_001003942.1; NM_001003942.1.
DR RefSeq; NP_001003943.1; NM_001003943.2.
DR RefSeq; NP_277038.1; NM_033503.3.
DR RefSeq; XP_005254814.1; XM_005254757.1.
DR RefSeq; XP_005254815.1; XM_005254758.1.
DR RefSeq; XP_005254816.1; XM_005254759.1.
DR RefSeq; XP_005254817.1; XM_005254760.1.
DR RefSeq; XP_005254818.1; XM_005254761.1.
DR RefSeq; XP_005254819.1; XM_005254762.1.
DR UniGene; Hs.591104; -.
DR ProteinModelPortal; Q96LC9; -.
DR IntAct; Q96LC9; 4.
DR STRING; 9606.ENSP00000346697; -.
DR PhosphoSite; Q96LC9; -.
DR PRIDE; Q96LC9; -.
DR DNASU; 90427; -.
DR Ensembl; ENST00000220446; ENSP00000220446; ENSG00000104081.
DR Ensembl; ENST00000354670; ENSP00000346697; ENSG00000104081.
DR Ensembl; ENST00000397573; ENSP00000380703; ENSG00000104081.
DR Ensembl; ENST00000431415; ENSP00000396511; ENSG00000104081.
DR Ensembl; ENST00000558774; ENSP00000453913; ENSG00000104081.
DR Ensembl; ENST00000559701; ENSP00000453919; ENSG00000104081.
DR Ensembl; ENST00000561282; ENSP00000453522; ENSG00000104081.
DR Ensembl; ENST00000561360; ENSP00000453892; ENSG00000104081.
DR GeneID; 90427; -.
DR KEGG; hsa:90427; -.
DR UCSC; uc001zkv.4; human.
DR CTD; 90427; -.
DR GeneCards; GC15M040380; -.
DR HGNC; HGNC:24132; BMF.
DR HPA; HPA010120; -.
DR MIM; 606266; gene.
DR neXtProt; NX_Q96LC9; -.
DR PharmGKB; PA134893658; -.
DR eggNOG; NOG40671; -.
DR HOVERGEN; HBG050697; -.
DR InParanoid; Q96LC9; -.
DR KO; K17460; -.
DR OMA; FHRLHMQ; -.
DR OrthoDB; EOG7QRQW6; -.
DR Reactome; REACT_578; Apoptosis.
DR GeneWiki; BMF_(gene); -.
DR GenomeRNAi; 90427; -.
DR NextBio; 76756; -.
DR PRO; PR:Q96LC9; -.
DR ArrayExpress; Q96LC9; -.
DR Bgee; Q96LC9; -.
DR CleanEx; HS_BMF; -.
DR Genevestigator; Q96LC9; -.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0016459; C:myosin complex; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043276; P:anoikis; IDA:MGI.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0032464; P:positive regulation of protein homooligomerization; ISS:BHF-UCL.
DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISS:BHF-UCL.
DR InterPro; IPR028192; BMF.
DR PANTHER; PTHR32014; PTHR32014; 1.
DR Pfam; PF15185; BMF; 1.
DR PROSITE; PS50062; BCL2_FAMILY; FALSE_NEG.
DR PROSITE; PS01259; BH3; FALSE_NEG.
PE 2: Evidence at transcript level;
KW Alternative splicing; Apoptosis; Complete proteome;
KW Reference proteome.
FT CHAIN 1 184 Bcl-2-modifying factor.
FT /FTId=PRO_0000143111.
FT REGION 67 75 Interaction with DLC2 (By similarity).
FT MOTIF 133 147 BH3.
FT VAR_SEQ 98 129 GNAGYRLPLPASFPAVLPIGEQPPEGQWQHQA -> APAEP
FT KSCVVADPPLPAQPCFEWRREQERGRP (in isoform
FT 3).
FT /FTId=VSP_012293.
FT VAR_SEQ 130 184 Missing (in isoform 3).
FT /FTId=VSP_012294.
FT VAR_SEQ 131 151 Missing (in isoform 2).
FT /FTId=VSP_012292.
FT CONFLICT 61 61 R -> Q (in Ref. 4; AAH69328).
FT CONFLICT 80 80 Q -> P (in Ref. 4; AAH69505).
SQ SEQUENCE 184 AA; 20508 MW; 21479B25CC727853 CRC64;
MEPSQCVEEL EDDVFQPEDG EPVTQPGSLL SADLFAQSLL DCPLSRLQLF PLTHCCGPGL
RPTSQEDKAT QTLSPASPSQ GVMLPCGVTE EPQRLFYGNA GYRLPLPASF PAVLPIGEQP
PEGQWQHQAE VQIARKLQCI ADQFHRLHVQ QHQQNQNRVW WQILLFLHNL ALNGEENRNG
AGPR
//
MIM
606266
*RECORD*
*FIELD* NO
606266
*FIELD* TI
*606266 BCL2-MODIFYING FACTOR; BMF
*FIELD* TX
DESCRIPTION
The BH3-only proteins, of which BMF is one, are proapoptotic members of
read morethe BCL2 (151430) family that share with their relatives only the short
BH3 domain, which allows their interaction with prosurvival BCL2 family
members to trigger apoptosis.
CLONING
Puthalakath et al. (2001) isolated mouse bmf using mouse Mcl1 (159552),
an antiapoptotic Bcl2 family member, as bait for a yeast 2-hybrid screen
of mouse embryo cDNA library. They cloned human BMF from a T lymphocyte
cDNA library using a mouse bmf cDNA as a probe. The deduced 184-amino
acid protein shares 87% sequence identity with the mouse protein. BMF
has a BH3 domain most similar to that found in BIM (603827), BIK
(603392), and EGL1.
GENE FUNCTION
Puthalakath et al. (2001) showed that BMF is sequestered to myosin V
(160777) motors by association with dynein light chain-2 (DLC2). Certain
damage signals, such as loss of cell attachment (anoikis), unleash BMF,
allowing it to translocate and bind prosurvival BCL2 proteins.
Puthalakath et al. (2001) concluded that at least 2 mammalian BH3-only
proteins, BMF and BIM, function to sense intracellular damage by their
localization to distinct cytoskeletal structures. A sequence in BMF
starting at aspartic acid-67 and continuing KATQTLSP closely resembles
the region in BIM (amino acids aspartic acid-51, KSTQTPSP) that mediates
its binding to DLC1 (601562). Mutations within this domain of BMF
abrogated the interaction of BMF with DLC2 in yeast and in mammalian
cells.
MAPPING
Puthalakath et al. (2001) mapped the BMF gene to chromosome 15q14, the
site of a candidate tumor suppressor gene lost in many metastatic, but
not primary, carcinomas.
*FIELD* RF
1. Puthalakath, H.; Villunger, A.; O'Reilly, L. A.; Beaumont, J. G.;
Coultas, L.; Cheney, R. E.; Huang, D. C. S.; Strasser, A.: Bmf: a
proapoptotic BH3-only protein regulated by interaction with the myosin
V actin motor complex, activated by anoikis. Science 293: 1829-1832,
2001. Note: Erratum: Science 297: 1122 only, 2002.
*FIELD* CD
Ada Hamosh: 9/17/2001
*FIELD* ED
alopez: 09/27/2004
carol: 7/10/2003
alopez: 9/17/2001
*RECORD*
*FIELD* NO
606266
*FIELD* TI
*606266 BCL2-MODIFYING FACTOR; BMF
*FIELD* TX
DESCRIPTION
The BH3-only proteins, of which BMF is one, are proapoptotic members of
read morethe BCL2 (151430) family that share with their relatives only the short
BH3 domain, which allows their interaction with prosurvival BCL2 family
members to trigger apoptosis.
CLONING
Puthalakath et al. (2001) isolated mouse bmf using mouse Mcl1 (159552),
an antiapoptotic Bcl2 family member, as bait for a yeast 2-hybrid screen
of mouse embryo cDNA library. They cloned human BMF from a T lymphocyte
cDNA library using a mouse bmf cDNA as a probe. The deduced 184-amino
acid protein shares 87% sequence identity with the mouse protein. BMF
has a BH3 domain most similar to that found in BIM (603827), BIK
(603392), and EGL1.
GENE FUNCTION
Puthalakath et al. (2001) showed that BMF is sequestered to myosin V
(160777) motors by association with dynein light chain-2 (DLC2). Certain
damage signals, such as loss of cell attachment (anoikis), unleash BMF,
allowing it to translocate and bind prosurvival BCL2 proteins.
Puthalakath et al. (2001) concluded that at least 2 mammalian BH3-only
proteins, BMF and BIM, function to sense intracellular damage by their
localization to distinct cytoskeletal structures. A sequence in BMF
starting at aspartic acid-67 and continuing KATQTLSP closely resembles
the region in BIM (amino acids aspartic acid-51, KSTQTPSP) that mediates
its binding to DLC1 (601562). Mutations within this domain of BMF
abrogated the interaction of BMF with DLC2 in yeast and in mammalian
cells.
MAPPING
Puthalakath et al. (2001) mapped the BMF gene to chromosome 15q14, the
site of a candidate tumor suppressor gene lost in many metastatic, but
not primary, carcinomas.
*FIELD* RF
1. Puthalakath, H.; Villunger, A.; O'Reilly, L. A.; Beaumont, J. G.;
Coultas, L.; Cheney, R. E.; Huang, D. C. S.; Strasser, A.: Bmf: a
proapoptotic BH3-only protein regulated by interaction with the myosin
V actin motor complex, activated by anoikis. Science 293: 1829-1832,
2001. Note: Erratum: Science 297: 1122 only, 2002.
*FIELD* CD
Ada Hamosh: 9/17/2001
*FIELD* ED
alopez: 09/27/2004
carol: 7/10/2003
alopez: 9/17/2001