Bcl-2-like protein 1 is a protein encoded in humans by the BCL2L1gene. Through
alternative splicing, the gene encodes both of the human proteins
Bcl-xL and
Bcl-xS.[5]
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 proteins encoded by this gene are located at the
outer mitochondrial membrane, and have been shown to regulate outer mitochondrial membrane channel (
voltage-dependent anion channels (VDACs) opening. VDACs regulate mitochondrial membrane potential, and thus controls the production of
reactive oxygen species and release of
cytochrome C by mitochondria, both of which are the potent inducers of
cell apoptosis. Two alternatively spliced transcript variants, which encode distinct isoforms, have been reported. The longer isoform (
Bcl-xL) acts as an apoptotic inhibitor and the shorter form (Bcl-xS) acts as an apoptotic activator.[5][6]
Interactions
BCL2-like 1 (gene) has been shown to
interact with:
^
abcRual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8.
Bibcode:
2005Natur.437.1173R.
doi:
10.1038/nature04209.
PMID16189514.
S2CID4427026.
^
abcdZhang H, Nimmer P, Rosenberg SH, Ng SC, Joseph M (Aug 2002). "Development of a high-throughput fluorescence polarization assay for Bcl-x(L)". Analytical Biochemistry. 307 (1): 70–5.
doi:
10.1016/S0003-2697(02)00028-3.
PMID12137781.
^
abcWhitfield J, Harada K, Bardelle C, Staddon JM (Nov 2003). "High-throughput methods to detect dimerization of Bcl-2 family proteins". Analytical Biochemistry. 322 (2): 170–8.
doi:
10.1016/j.ab.2003.07.014.
PMID14596824.
^Degterev A, Lugovskoy A, Cardone M, Mulley B, Wagner G, Mitchison T, Yuan J (Feb 2001). "Identification of small-molecule inhibitors of interaction between the BH3 domain and Bcl-xL". Nature Cell Biology. 3 (2): 173–82.
doi:
10.1038/35055085.
PMID11175750.
S2CID32934759.
^Qin W, Hu J, Guo M, Xu J, Li J, Yao G, Zhou X, Jiang H, Zhang P, Shen L, Wan D, Gu J (Aug 2003). "BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis". Biochemical and Biophysical Research Communications. 308 (2): 379–85.
doi:
10.1016/S0006-291X(03)01387-1.
PMID12901880.
^Yasuda M, Han JW, Dionne CA, Boyd JM, Chinnadurai G (Feb 1999). "BNIP3alpha: a human homolog of mitochondrial proapoptotic protein BNIP3". Cancer Research. 59 (3): 533–7.
PMID9973195.
^
abKomatsu K, Miyashita T, Hang H, Hopkins KM, Zheng W, Cuddeback S, Yamada M, Lieberman HB, Wang HG (Jan 2000). "Human homologue of S. pombe Rad9 interacts with BCL-2/BCL-xL and promotes apoptosis". Nature Cell Biology. 2 (1): 1–6.
doi:
10.1038/71316.
PMID10620799.
S2CID52847351.
^
abStrobel T, Tai YT, Korsmeyer S, Cannistra SA (Nov 1998). "BAD partly reverses paclitaxel resistance in human ovarian cancer cells". Oncogene. 17 (19): 2419–27.
doi:
10.1038/sj.onc.1202180.
PMID9824152.
S2CID44240363.
^Oda E, Ohki R, Murasawa H, Nemoto J, Shibue T, Yamashita T, Tokino T, Taniguchi T, Tanaka N (May 2000). "Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis". Science. 288 (5468): 1053–8.
Bibcode:
2000Sci...288.1053O.
doi:
10.1126/science.288.5468.1053.
PMID10807576.
^Shi Y, Chen J, Weng C, Chen R, Zheng Y, Chen Q, Tang H (Jun 2003). "Identification of the protein-protein contact site and interaction mode of human VDAC1 with Bcl-2 family proteins". Biochemical and Biophysical Research Communications. 305 (4): 989–96.
doi:
10.1016/S0006-291X(03)00871-4.
PMID12767928.
Ogata Y, Takahashi M (Sep 2003). "Bcl-xL as an antiapoptotic molecule for cardiomyocytes". Drug News & Perspectives. 16 (7): 446–52.
doi:
10.1358/dnp.2003.16.7.829356.
PMID14668940.
Bcl-2-like protein 1 is a protein encoded in humans by the BCL2L1gene. Through
alternative splicing, the gene encodes both of the human proteins
Bcl-xL and
Bcl-xS.[5]
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 proteins encoded by this gene are located at the
outer mitochondrial membrane, and have been shown to regulate outer mitochondrial membrane channel (
voltage-dependent anion channels (VDACs) opening. VDACs regulate mitochondrial membrane potential, and thus controls the production of
reactive oxygen species and release of
cytochrome C by mitochondria, both of which are the potent inducers of
cell apoptosis. Two alternatively spliced transcript variants, which encode distinct isoforms, have been reported. The longer isoform (
Bcl-xL) acts as an apoptotic inhibitor and the shorter form (Bcl-xS) acts as an apoptotic activator.[5][6]
Interactions
BCL2-like 1 (gene) has been shown to
interact with:
^
abcRual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8.
Bibcode:
2005Natur.437.1173R.
doi:
10.1038/nature04209.
PMID16189514.
S2CID4427026.
^
abcdZhang H, Nimmer P, Rosenberg SH, Ng SC, Joseph M (Aug 2002). "Development of a high-throughput fluorescence polarization assay for Bcl-x(L)". Analytical Biochemistry. 307 (1): 70–5.
doi:
10.1016/S0003-2697(02)00028-3.
PMID12137781.
^
abcWhitfield J, Harada K, Bardelle C, Staddon JM (Nov 2003). "High-throughput methods to detect dimerization of Bcl-2 family proteins". Analytical Biochemistry. 322 (2): 170–8.
doi:
10.1016/j.ab.2003.07.014.
PMID14596824.
^Degterev A, Lugovskoy A, Cardone M, Mulley B, Wagner G, Mitchison T, Yuan J (Feb 2001). "Identification of small-molecule inhibitors of interaction between the BH3 domain and Bcl-xL". Nature Cell Biology. 3 (2): 173–82.
doi:
10.1038/35055085.
PMID11175750.
S2CID32934759.
^Qin W, Hu J, Guo M, Xu J, Li J, Yao G, Zhou X, Jiang H, Zhang P, Shen L, Wan D, Gu J (Aug 2003). "BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis". Biochemical and Biophysical Research Communications. 308 (2): 379–85.
doi:
10.1016/S0006-291X(03)01387-1.
PMID12901880.
^Yasuda M, Han JW, Dionne CA, Boyd JM, Chinnadurai G (Feb 1999). "BNIP3alpha: a human homolog of mitochondrial proapoptotic protein BNIP3". Cancer Research. 59 (3): 533–7.
PMID9973195.
^
abKomatsu K, Miyashita T, Hang H, Hopkins KM, Zheng W, Cuddeback S, Yamada M, Lieberman HB, Wang HG (Jan 2000). "Human homologue of S. pombe Rad9 interacts with BCL-2/BCL-xL and promotes apoptosis". Nature Cell Biology. 2 (1): 1–6.
doi:
10.1038/71316.
PMID10620799.
S2CID52847351.
^
abStrobel T, Tai YT, Korsmeyer S, Cannistra SA (Nov 1998). "BAD partly reverses paclitaxel resistance in human ovarian cancer cells". Oncogene. 17 (19): 2419–27.
doi:
10.1038/sj.onc.1202180.
PMID9824152.
S2CID44240363.
^Oda E, Ohki R, Murasawa H, Nemoto J, Shibue T, Yamashita T, Tokino T, Taniguchi T, Tanaka N (May 2000). "Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis". Science. 288 (5468): 1053–8.
Bibcode:
2000Sci...288.1053O.
doi:
10.1126/science.288.5468.1053.
PMID10807576.
^Shi Y, Chen J, Weng C, Chen R, Zheng Y, Chen Q, Tang H (Jun 2003). "Identification of the protein-protein contact site and interaction mode of human VDAC1 with Bcl-2 family proteins". Biochemical and Biophysical Research Communications. 305 (4): 989–96.
doi:
10.1016/S0006-291X(03)00871-4.
PMID12767928.
Ogata Y, Takahashi M (Sep 2003). "Bcl-xL as an antiapoptotic molecule for cardiomyocytes". Drug News & Perspectives. 16 (7): 446–52.
doi:
10.1358/dnp.2003.16.7.829356.
PMID14668940.