BCL2L11: Difference between revisions

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Latest revision as of 14:26, 28 January 2018

Bcl-2-like protein 11, commonly called BIM, is a protein that in humans is encoded by the BCL2L11 gene.^[1]^[2]

Function

The protein encoded by this gene belongs to the BCL-2 protein family. BCL-2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. The protein encoded by this gene contains a Bcl-2 homology domain 3 (BH3). It has been shown to interact with other members of the BCL-2 protein family, including BCL2, BCL2L1/BCL-X(L), and MCL1, and to act as an apoptotic activator. The expression of this gene can be induced by nerve growth factor (NGF), as well as by the forkhead transcription factor FKHR-L1 (FoxO3a), which suggests a role of this gene in neuronal and lymphocyte apoptosis. Transgenic studies of the mouse counterpart suggested that this gene functions as an essential initiator of apoptosis in thymocyte-negative selection. Several alternatively spliced transcript variants of this gene have been identified.^[3]

Regulation of Bim

Bim expression and activity are regulated at the transcriptional, translational and post-translational levels; coordinated expression and activity of Bim shape immune responses, and ensure tissue integrity. Cancer cells develop mechanisms that suppress Bim expression, which allows for tumor progression and metastasis.^[4]

Interactions

BCL2L11 has been shown to interact with:

References

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 Hsu SY, Lin P, Hsueh AJ (November 1998). "BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members". Mol Endocrinol. 12 (9): 1432–40. doi:10.1210/mend.12.9.0166. PMID 9731710.
↑ ^2.0 ^2.1 ^2.2 ^2.3 O'Connor L, Strasser A, O'Reilly LA, Hausmann G, Adams JM, Cory S, Huang DC (February 1998). "Bim: a novel member of the Bcl-2 family that promotes apoptosis". EMBO J. 17 (2): 384–95. doi:10.1093/emboj/17.2.384. PMC 1170389. PMID 9430630.
↑ "Entrez Gene: BCL2L11 BCL2-like 11 (apoptosis facilitator)".
↑ Sionov RV, Vlahopoulos SA, Granot Z (2015). "Regulation of Bim in Health and Disease". Oncotarget. 6 (27): 23058–134. doi:10.18632/oncotarget.5492. PMC 4695108. PMID 26405162.
↑ ^5.0 ^5.1 ^5.2 Chen L, Willis SN, Wei A, Smith BJ, Fletcher JI, Hinds MG, Colman PM, Day CL, Adams JM, Huang DC (February 2005). "Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function". Mol. Cell. 17 (3): 393–403. doi:10.1016/j.molcel.2004.12.030. PMID 15694340.
↑ Whitfield J, Harada K, Bardelle C, Staddon JM (November 2003). "High-throughput methods to detect dimerization of Bcl-2 family proteins". Anal. Biochem. 322 (2): 170–8. doi:10.1016/j.ab.2003.07.014. PMID 14596824.
↑ Day CL, Puthalakath H, Skea G, Strasser A, Barsukov I, Lian LY, Huang DC, Hinds MG (February 2004). "Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands". Biochem. J. 377 (Pt 3): 597–605. doi:10.1042/BJ20031251. PMC 1223895. PMID 14561217.
↑ Vadlamudi RK, Bagheri-Yarmand R, Yang Z, Balasenthil S, Nguyen D, Sahin AA, den Hollander P, Kumar R (June 2004). "Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes". Cancer Cell. 5 (6): 575–85. doi:10.1016/j.ccr.2004.05.022. PMID 15193260.
↑ Bae J, Leo CP, Hsu SY, Hsueh AJ (August 2000). "MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain". J. Biol. Chem. 275 (33): 25255–61. doi:10.1074/jbc.M909826199. PMID 10837489.

External links

BCL2L11 human gene location in the UCSC Genome Browser.
BCL2L11 human gene details in the UCSC Genome Browser.

This article on a gene on human chromosome 2 is a stub. You can help Wikipedia by expanding it.

[pmid9731710-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 Hsu SY, Lin P, Hsueh AJ (November 1998). "BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members". Mol Endocrinol. 12 (9): 1432–40. doi:10.1210/mend.12.9.0166. PMID 9731710.

[pmid9430630-2] 2.0 ^2.1 ^2.2 ^2.3 O'Connor L, Strasser A, O'Reilly LA, Hausmann G, Adams JM, Cory S, Huang DC (February 1998). "Bim: a novel member of the Bcl-2 family that promotes apoptosis". EMBO J. 17 (2): 384–95. doi:10.1093/emboj/17.2.384. PMC 1170389. PMID 9430630.

[3] "Entrez Gene: BCL2L11 BCL2-like 11 (apoptosis facilitator)".

[pmid26405162-4] Sionov RV, Vlahopoulos SA, Granot Z (2015). "Regulation of Bim in Health and Disease". Oncotarget. 6 (27): 23058–134. doi:10.18632/oncotarget.5492. PMC 4695108. PMID 26405162.

[pmid15694340-5] 5.0 ^5.1 ^5.2 Chen L, Willis SN, Wei A, Smith BJ, Fletcher JI, Hinds MG, Colman PM, Day CL, Adams JM, Huang DC (February 2005). "Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function". Mol. Cell. 17 (3): 393–403. doi:10.1016/j.molcel.2004.12.030. PMID 15694340.

[pmid14596824-6] Whitfield J, Harada K, Bardelle C, Staddon JM (November 2003). "High-throughput methods to detect dimerization of Bcl-2 family proteins". Anal. Biochem. 322 (2): 170–8. doi:10.1016/j.ab.2003.07.014. PMID 14596824.

[pmid14561217-7] Day CL, Puthalakath H, Skea G, Strasser A, Barsukov I, Lian LY, Huang DC, Hinds MG (February 2004). "Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands". Biochem. J. 377 (Pt 3): 597–605. doi:10.1042/BJ20031251. PMC 1223895. PMID 14561217.

[pmid15193260-8] Vadlamudi RK, Bagheri-Yarmand R, Yang Z, Balasenthil S, Nguyen D, Sahin AA, den Hollander P, Kumar R (June 2004). "Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes". Cancer Cell. 5 (6): 575–85. doi:10.1016/j.ccr.2004.05.022. PMID 15193260.

[pmid10837489-9] Bae J, Leo CP, Hsu SY, Hsueh AJ (August 2000). "MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain". J. Biol. Chem. 275 (33): 25255–61. doi:10.1074/jbc.M909826199. PMID 10837489.

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@@ Line 1: / Line 1: @@
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Infobox_gene}}
-{{PBB_Controls
+'''Bcl-2-like protein 11''', commonly called BIM, is a [[protein]] that in humans is encoded by the ''BCL2L11'' [[gene]].<ref name="pmid9731710">{{cite journal | vauthors = Hsu SY, Lin P, Hsueh AJ | title = BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members | journal = Mol Endocrinol | volume = 12 | issue = 9 | pages = 1432–40 | date=November 1998| pmid = 9731710 | pmc =  | doi =10.1210/mend.12.9.0166  }}</ref><ref name="pmid9430630">{{cite journal | vauthors = O'Connor L, Strasser A, O'Reilly LA, Hausmann G, Adams JM, Cory S, Huang DC | title = Bim: a novel member of the Bcl-2 family that promotes apoptosis | journal = EMBO J | volume = 17 | issue = 2 | pages = 384–95 | date=February 1998| pmid = 9430630 | pmc = 1170389 | doi = 10.1093/emboj/17.2.384 }}</ref>
-| update_page = yes
-| require_manual_inspection = no
-| update_protein_box = yes
-| update_summary = yes
-| update_citations = yes
-}}
-<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+== Function ==
-{{GNF_Protein_box
- | image =
- | image_source =
- | PDB =
- | Name = BCL2-like 11 (apoptosis facilitator)
- | HGNCid = 994
- | Symbol = BCL2L11
- | AltSymbols =; BAM; BIM; BIM-alpha6; BIM-beta6; BIM-beta7; BOD; BimEL; BimL
- | OMIM = 603827
- | ECnumber =
- | Homologene = 7643
- | MGIid = 1197519
- | GeneAtlas_image1 = PBB_GE_BCL2L11_208536_s_at_tn.png
- | GeneAtlas_image2 = PBB_GE_BCL2L11_222343_at_tn.png
- | Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
- | Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0016020 |text = membrane}}
- | Process = {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0043065 |text = positive regulation of apoptosis}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 10018
-    | Hs_Ensembl = ENSG00000153094
-    | Hs_RefseqProtein = NP_619528
-    | Hs_RefseqmRNA = NM_138622
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 2
-    | Hs_GenLoc_start = 111597781
-    | Hs_GenLoc_end = 111641054
-    | Hs_Uniprot = O43521
-    | Mm_EntrezGene = 12125
-    | Mm_Ensembl = ENSMUSG00000027381
-    | Mm_RefseqmRNA = NM_009754
-    | Mm_RefseqProtein = NP_033884
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 2
-    | Mm_GenLoc_start = 127817479
-    | Mm_GenLoc_end = 127853613
-    | Mm_Uniprot = Q542N5
-  }}
-}}
-'''BCL2-like 11 (apoptosis facilitator)''', also known as '''BCL2L11''', is a human [[gene]].
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+The protein encoded by this gene belongs to the [[Bcl-2 family|BCL-2]] protein family. BCL-2 family members form hetero- or homodimers and act as anti- or pro-[[apoptotic]] regulators that are involved in a wide variety of cellular activities. The protein encoded by this gene contains a Bcl-2 homology domain 3 (BH3). It has been shown to interact with other members of the BCL-2 protein family, including [[BCL2]], [[BCL2L1]]/BCL-X(L), and [[MCL1]], and to act as an apoptotic activator. The expression of this gene can be induced by [[nerve growth factor]] (NGF), as well as by the forkhead transcription factor FKHR-L1 ([[FOXO3|FoxO3a]]), which suggests a role of this gene in neuronal and lymphocyte apoptosis. Transgenic studies of the mouse counterpart suggested that this gene functions as an essential initiator of apoptosis in [[thymocyte]]-negative selection. Several alternatively spliced transcript variants of this gene have been identified.<ref>{{cite web | title = Entrez Gene: BCL2L11 BCL2-like 11 (apoptosis facilitator)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10018| accessdate = }}</ref>
-{{PBB_Summary
-| section_title =
+=== Regulation of Bim ===
-| summary_text = The protein encoded by this gene belongs to the BCL-2 protein family. BCL-2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. The protein encoded by this gene contains a Bcl-2 homology domain 3 (BH3). It has been shown to interact with other members of the BCL-2 protein family, including BCL2, BCL2L1/BCL-X(L), and MCL1, and to act as an apoptotic activator. The expression of this gene can be induced by nerve growth factor (NGF), as well as by the forkhead transcription factor FKHR-L1, which suggests a role of this gene in neuronal and lymphocyte apoptosis. Transgenic studies of the mouse counterpart suggested that this gene functions as an essential initiator of apoptosis in thymocyte-negative selection. Several alternatively spliced transcript variants of this gene have been identified.<ref>{{cite web | title = Entrez Gene: BCL2L11 BCL2-like 11 (apoptosis facilitator)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10018| accessdate = }}</ref>
-}}
+Bim expression and activity are regulated at the transcriptional, translational and post-translational levels; coordinated expression and activity of Bim shape immune responses, and ensure tissue integrity. Cancer cells develop mechanisms that suppress Bim expression, which allows for tumor progression and metastasis.<ref name="pmid26405162">{{cite journal |vauthors = Sionov RV, Vlahopoulos SA, Granot Z |title = Regulation of Bim in Health and Disease |journal = Oncotarget |volume = 6 |issue = 27 |pages = 23058–134 |year = 2015 |pmid = 26405162 |pmc = 4695108 |doi = 10.18632/oncotarget.5492 }}</ref>
+== Interactions ==
+BCL2L11 has been shown to [[Protein-protein interaction|interact]] with:
+* [[BCL2-like 1 (gene)|BCL2-like 1]],<ref name = pmid9731710/><ref name = pmid9430630 /><ref name = pmid15694340/><ref name = pmid14596824>{{cite journal | date = November 2003 | vauthors = Whitfield J, Harada K, Bardelle C, Staddon JM | title = High-throughput methods to detect dimerization of Bcl-2 family proteins | journal = Anal. Biochem. | volume = 322 | issue = 2 | pages = 170–8 | pmid = 14596824 | doi = 10.1016/j.ab.2003.07.014}}</ref>
+* [[BCL2L2]],<ref name = pmid9731710/><ref name = pmid9430630/>
+* [[Bcl-2]],<ref name = pmid9731710/><ref name = pmid9430630/><ref name = pmid15694340/>
+* [[DYNLL1]],<ref name = pmid14561217>{{cite journal | date = February 2004 | vauthors = Day CL, Puthalakath H, Skea G, Strasser A, Barsukov I, Lian LY, Huang DC, Hinds MG | title = Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands | journal = Biochem. J. | volume = 377 | issue = Pt 3 | pages = 597–605 | pmid = 14561217 | pmc = 1223895 | doi = 10.1042/BJ20031251}}</ref><ref name = pmid15193260>{{cite journal | date = June 2004 | vauthors = Vadlamudi RK, Bagheri-Yarmand R, Yang Z, Balasenthil S, Nguyen D, Sahin AA, den Hollander P, Kumar R | title = Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes | journal = Cancer Cell | volume = 5 | issue = 6 | pages = 575–85 | pmid = 15193260 | doi = 10.1016/j.ccr.2004.05.022}}</ref>  and
+* [[MCL1]].<ref name = pmid9731710 /><ref name = pmid15694340>{{cite journal | date = February 2005 | vauthors = Chen L, Willis SN, Wei A, Smith BJ, Fletcher JI, Hinds MG, Colman PM, Day CL, Adams JM, Huang DC | title = Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function | journal = Mol. Cell | volume = 17 | issue = 3 | pages = 393–403 | pmid = 15694340 | doi = 10.1016/j.molcel.2004.12.030}}</ref><ref name = pmid10837489>{{cite journal | date = August 2000 | vauthors = Bae J, Leo CP, Hsu SY, Hsueh AJ | title = MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain | journal = J. Biol. Chem. | volume = 275 | issue = 33 | pages = 25255–61 | pmid = 10837489 | doi = 10.1074/jbc.M909826199}}</ref>
 ==See also==
 * [[Bcl-2]]
-==References==
+== References ==
-{{reflist|2}}
+{{reflist}}
-==Further reading==
+== Further reading ==
 {{refbegin | 2}}
-{{PBB_Further_reading
+*{{cite journal  | vauthors=Wang K, Yin XM, Chao DT |title=BID: a novel BH3 domain-only death agonist |journal=Genes Dev. |volume=10 |issue= 22 |pages= 2859–69 |year= 1996 |pmid= 8918887 |doi=10.1101/gad.10.22.2859  |display-authors=etal}}
-| citations =
+*{{cite journal  | vauthors=Zha J, Harada H, Yang E |title=Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L) |journal=Cell |volume=87 |issue= 4 |pages= 619–28 |year= 1997 |pmid= 8929531 |doi=10.1016/S0092-8674(00)81382-3  |display-authors=etal}}
-*{{cite journal  | author=Wang K, Yin XM, Chao DT, ''et al.'' |title=BID: a novel BH3 domain-only death agonist. |journal=Genes Dev. |volume=10 |issue= 22 |pages= 2859-69 |year= 1996 |pmid= 8918887 |doi=  }}
+*{{cite journal  | vauthors=Huang DC, Adams JM, Cory S |title=The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4 |journal=EMBO J. |volume=17 |issue= 4 |pages= 1029–39 |year= 1998 |pmid= 9463381 |doi= 10.1093/emboj/17.4.1029  | pmc=1170452 }}
-*{{cite journal  | author=Zha J, Harada H, Yang E, ''et al.'' |title=Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L) |journal=Cell |volume=87 |issue= 4 |pages= 619-28 |year= 1997 |pmid= 8929531 |doi=  }}
+*{{cite journal  | vauthors=Puthalakath H, Huang DC, O'Reilly LA |title=The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex |journal=Mol. Cell |volume=3 |issue= 3 |pages= 287–96 |year= 1999 |pmid= 10198631 |doi=10.1016/S1097-2765(00)80456-6  |display-authors=etal}}
-*{{cite journal  | author=O'Connor L, Strasser A, O'Reilly LA, ''et al.'' |title=Bim: a novel member of the Bcl-2 family that promotes apoptosis. |journal=EMBO J. |volume=17 |issue= 2 |pages= 384-95 |year= 1998 |pmid= 9430630 |doi= 10.1093/emboj/17.2.384 }}
+*{{cite journal  | vauthors=Ohi N, Tokunaga A, Tsunoda H |title=A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis induced by Nip3 by forming a heterodimer through the C-terminal hydrophobic region |journal=Cell Death Differ. |volume=6 |issue= 4 |pages= 314–25 |year= 1999 |pmid= 10381623 |doi= 10.1038/sj.cdd.4400493 |display-authors=etal}}
-*{{cite journal  | author=Huang DC, Adams JM, Cory S |title=The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4. |journal=EMBO J. |volume=17 |issue= 4 |pages= 1029-39 |year= 1998 |pmid= 9463381 |doi= 10.1093/emboj/17.4.1029 }}
+*{{cite journal  | vauthors=Bouillet P, Metcalf D, Huang DC |title=Proapoptotic Bcl-2 relative Bim required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity |journal=Science |volume=286 |issue= 5445 |pages= 1735–8 |year= 1999 |pmid= 10576740 |doi=10.1126/science.286.5445.1735  |display-authors=etal}}
-*{{cite journal  | author=Hsu SY, Lin P, Hsueh AJ |title=BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members. |journal=Mol. Endocrinol. |volume=12 |issue= 9 |pages= 1432-40 |year= 1998 |pmid= 9731710 |doi=  }}
+*{{cite journal  | vauthors=Dijkers PF, Medema RH, Lammers JW |title=Expression of the pro-apoptotic Bcl-2 family member Bim is regulated by the forkhead transcription factor FKHR-L1 |journal=Curr. Biol. |volume=10 |issue= 19 |pages= 1201–4 |year= 2000 |pmid= 11050388 |doi=10.1016/S0960-9822(00)00728-4  |display-authors=etal}}
-*{{cite journal  | author=Puthalakath H, Huang DC, O'Reilly LA, ''et al.'' |title=The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. |journal=Mol. Cell |volume=3 |issue= 3 |pages= 287-96 |year= 1999 |pmid= 10198631 |doi=  }}
+*{{cite journal  | vauthors=Bouillet P, Zhang LC, Huang DC |title=Gene structure alternative splicing, and chromosomal localization of pro-apoptotic Bcl-2 relative Bim |journal=Mamm. Genome |volume=12 |issue= 2 |pages= 163–8 |year= 2001 |pmid= 11210187 |doi=10.1007/s003350010242  |display-authors=etal}}
-*{{cite journal  | author=Ohi N, Tokunaga A, Tsunoda H, ''et al.'' |title=A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis induced by Nip3 by forming a heterodimer through the C-terminal hydrophobic region. |journal=Cell Death Differ. |volume=6 |issue= 4 |pages= 314-25 |year= 1999 |pmid= 10381623 |doi= 10.1038/sj.cdd.4400493 }}
+*{{cite journal  | vauthors=Putcha GV, Moulder KL, Golden JP |title=Induction of BIM, a proapoptotic BH3-only BCL-2 family member, is critical for neuronal apoptosis |journal=Neuron |volume=29 |issue= 3 |pages= 615–28 |year= 2001 |pmid= 11301022 |doi=10.1016/S0896-6273(01)00238-0  |display-authors=etal}}
-*{{cite journal  | author=Bouillet P, Metcalf D, Huang DC, ''et al.'' |title=Proapoptotic Bcl-2 relative Bim required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity. |journal=Science |volume=286 |issue= 5445 |pages= 1735-8 |year= 1999 |pmid= 10576740 |doi=  }}
+*{{cite journal  | vauthors=Murray S, Halford S, Ebenezer ND |title=Assignment of BCL2L11 to human chromosome band 2p13 with somatic cell and radiation hybrids |journal=Cytogenet. Cell Genet. |volume=92 |issue= 3–4 |pages= 353 |year= 2001 |pmid= 11435715 |doi=10.1159/000056930  |display-authors=etal}}
-*{{cite journal  | author=Bae J, Leo CP, Hsu SY, Hsueh AJ |title=MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain. |journal=J. Biol. Chem. |volume=275 |issue= 33 |pages= 25255-61 |year= 2000 |pmid= 10837489 |doi= 10.1074/jbc.M909826199 }}
+*{{cite journal  | vauthors=Cheng EH, Wei MC, Weiler S |title=BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis |journal=Mol. Cell |volume=8 |issue= 3 |pages= 705–11 |year= 2001 |pmid= 11583631 |doi=10.1016/S1097-2765(01)00320-3  |display-authors=etal}}
-*{{cite journal  | author=Dijkers PF, Medema RH, Lammers JW, ''et al.'' |title=Expression of the pro-apoptotic Bcl-2 family member Bim is regulated by the forkhead transcription factor FKHR-L1. |journal=Curr. Biol. |volume=10 |issue= 19 |pages= 1201-4 |year= 2000 |pmid= 11050388 |doi=  }}
+*{{cite journal  | vauthors=Mami U, Miyashita T, Shikama Y |title=Molecular cloning and characterization of six novel isoforms of human Bim, a member of the proapoptotic Bcl-2 family |journal=FEBS Lett. |volume=509 |issue= 1 |pages= 135–41 |year= 2002 |pmid= 11734221 |doi=10.1016/S0014-5793(01)03145-3  |display-authors=etal}}
-*{{cite journal  | author=Bouillet P, Zhang LC, Huang DC, ''et al.'' |title=Gene structure alternative splicing, and chromosomal localization of pro-apoptotic Bcl-2 relative Bim. |journal=Mamm. Genome |volume=12 |issue= 2 |pages= 163-8 |year= 2001 |pmid= 11210187 |doi=  }}
+*{{cite journal  | vauthors=Bouillet P, Purton JF, Godfrey DI |title=BH3-only Bcl-2 family member Bim is required for apoptosis of autoreactive thymocytes |journal=Nature |volume=415 |issue= 6874 |pages= 922–6 |year= 2002 |pmid= 11859372 |doi= 10.1038/415922a |display-authors=etal}}
-*{{cite journal  | author=Putcha GV, Moulder KL, Golden JP, ''et al.'' |title=Induction of BIM, a proapoptotic BH3-only BCL-2 family member, is critical for neuronal apoptosis. |journal=Neuron |volume=29 |issue= 3 |pages= 615-28 |year= 2001 |pmid= 11301022 |doi=  }}
+*{{cite journal  | vauthors=Marani M, Tenev T, Hancock D |title=Identification of novel isoforms of the BH3 domain protein Bim which directly activate Bax to trigger apoptosis |journal=Mol. Cell. Biol. |volume=22 |issue= 11 |pages= 3577–89 |year= 2002 |pmid= 11997495 |doi=10.1128/MCB.22.11.3577-3589.2002  | pmc=133811  |display-authors=etal}}
-*{{cite journal  | author=Murray S, Halford S, Ebenezer ND, ''et al.'' |title=Assignment of BCL2L11 to human chromosome band 2p13 with somatic cell and radiation hybrids. |journal=Cytogenet. Cell Genet. |volume=92 |issue= 3-4 |pages= 353 |year= 2001 |pmid= 11435715 |doi=  }}
+*{{cite journal  | vauthors=Liu JW, Chandra D, Tang SH |title=Identification and characterization of Bimgamma, a novel proapoptotic BH3-only splice variant of Bim |journal=Cancer Res. |volume=62 |issue= 10 |pages= 2976–81 |year= 2002 |pmid= 12019181 |doi=  |display-authors=etal}}
-*{{cite journal  | author=Cheng EH, Wei MC, Weiler S, ''et al.'' |title=BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. |journal=Mol. Cell |volume=8 |issue= 3 |pages= 705-11 |year= 2001 |pmid= 11583631 |doi=  }}
+*{{cite journal  | vauthors=Terradillos O, Montessuit S, Huang DC, Martinou JC |title=Direct addition of BimL to mitochondria does not lead to cytochrome c release |journal=FEBS Lett. |volume=522 |issue= 1–3 |pages= 29–34 |year= 2002 |pmid= 12095614 |doi=10.1016/S0014-5793(02)02871-5  }}
-*{{cite journal  | author=U M, Miyashita T, Shikama Y, ''et al.'' |title=Molecular cloning and characterization of six novel isoforms of human Bim, a member of the proapoptotic Bcl-2 family. |journal=FEBS Lett. |volume=509 |issue= 1 |pages= 135-41 |year= 2002 |pmid= 11734221 |doi=  }}
+*{{cite journal  | vauthors=Sugiyama T, Shimizu S, Matsuoka Y |title=Activation of mitochondrial voltage-dependent anion channel by apro-apoptotic BH3-only protein Bim |journal=Oncogene |volume=21 |issue= 32 |pages= 4944–56 |year= 2002 |pmid= 12118373 |doi= 10.1038/sj.onc.1205621 |display-authors=etal}}
-*{{cite journal  | author=Bouillet P, Purton JF, Godfrey DI, ''et al.'' |title=BH3-only Bcl-2 family member Bim is required for apoptosis of autoreactive thymocytes. |journal=Nature |volume=415 |issue= 6874 |pages= 922-6 |year= 2002 |pmid= 11859372 |doi= 10.1038/415922a }}
-*{{cite journal  | author=Marani M, Tenev T, Hancock D, ''et al.'' |title=Identification of novel isoforms of the BH3 domain protein Bim which directly activate Bax to trigger apoptosis. |journal=Mol. Cell. Biol. |volume=22 |issue= 11 |pages= 3577-89 |year= 2002 |pmid= 11997495 |doi=  }}
-*{{cite journal  | author=Liu JW, Chandra D, Tang SH, ''et al.'' |title=Identification and characterization of Bimgamma, a novel proapoptotic BH3-only splice variant of Bim. |journal=Cancer Res. |volume=62 |issue= 10 |pages= 2976-81 |year= 2002 |pmid= 12019181 |doi=  }}
-*{{cite journal  | author=Terradillos O, Montessuit S, Huang DC, Martinou JC |title=Direct addition of BimL to mitochondria does not lead to cytochrome c release. |journal=FEBS Lett. |volume=522 |issue= 1-3 |pages= 29-34 |year= 2002 |pmid= 12095614 |doi=  }}
-*{{cite journal  | author=Sugiyama T, Shimizu S, Matsuoka Y, ''et al.'' |title=Activation of mitochondrial voltage-dependent anion channel by apro-apoptotic BH3-only protein Bim. |journal=Oncogene |volume=21 |issue= 32 |pages= 4944-56 |year= 2002 |pmid= 12118373 |doi= 10.1038/sj.onc.1205621 }}
-}}
 {{refend}}
-{{protein-stub}}
+== External links ==
-{{WikiDoc Sources}}
+* {{UCSC genome browser|BCL2L11}}
+* {{UCSC gene details|BCL2L11}}
+{{gene-2-stub}}

BCL2L11: Difference between revisions

Latest revision as of 14:26, 28 January 2018

Contents

Function

Regulation of Bim

Interactions

See also

References

Further reading

External links

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