BCR (gen)

Oligomerizacijski domen onkoproteina Bcr-Abl
Oligomerizacijski domen onkoproteina Bcr-Abl
	Oligomerizacijski domen strukture onkoproteina bcr-abl
Identifikatori
Simbol	Bcr-Abl_Oligo

BCR
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	1K1F, 2AIN
Identifikatori
Aliasi	BCR
Vanjski ID-jevi	OMIM: 151410 MGI: 88141 HomoloGene: 3192 GeneCards: BCR
Lokacija gena (čovjek)
Hrom.	Hromosom 22 (čovjek)
Kraj	23,318,037 bp
Lokacija gena (miš)
Hrom.	Hromosom 10 (miš)
Kraj	75,020,753 bp
Ontologija gena
Molekularna funkcija	• aktivnost sa transferazom; • nucleotide binding; • guanyl-nucleotide exchange factor activity; • kinase activity; • protein serine/threonine kinase activity; • GO:0001948, GO:0016582 vezivanje za proteine; • vezivanje enzima; • protein tyrosine kinase activity; • ATP binding; • GO:0005097, GO:0005099, GO:0005100 GTPase activator activity;
Ćelijska komponenta	• citoplazma; • citosol; • postsynaptic membrane; • membrana; • GO:0097483, GO:0097481 postsynaptic density; • ćelijska membrana; • sinapsa; • međućelijske veze; • Egzosom; • GO:0009327 makromolekulani kompleks; • Schaffer collateral - CA1 synapse; • glutamatergic synapse; • postsynaptic density, intracellular component; • intracellular anatomical structure;
Biološki proces	• positive regulation of phagocytosis; • GO:0007243 intracellular signal transduction; • neuromuscular process controlling balance; • Fosforilacija; • regulation of cell cycle; • negative regulation of blood vessel remodeling; • protein phosphorylation; • negative regulation of cellular extravasation; • response to lipopolysaccharide; • brain development; • regulation of vascular permeability; • negative regulation of cell migration; • negative regulation of neutrophil degranulation; • inner ear morphogenesis; • protein autophosphorylation; • platelet-derived growth factor receptor signaling pathway; • regulation of Rho protein signal transduction; • regulation of small GTPase mediated signal transduction; • negative regulation of inflammatory response; • actin cytoskeleton organization; • GO:0072468 Transdukcija signala; • peptidyl-tyrosine phosphorylation; • renal system process; • homeostasis of number of cells; • regulation of nitrogen compound metabolic process; • definitive hemopoiesis; • negative regulation of respiratory burst; • intracellular protein transmembrane transport; • cellular response to lipopolysaccharide; • negative regulation of reactive oxygen species metabolic process; • GO:0032320, GO:0032321, GO:0032855, GO:0043089, GO:0032854 positive regulation of GTPase activity; • modulation of chemical synaptic transmission; • small GTPase mediated signal transduction; • keratinocyte differentiation; • focal adhesion assembly; • GO:0032861, GO:0032862, GO:0032856 activation of GTPase activity;
	Izvori:Amigo / QuickGO
Ortolozi
	613
	110279
	ENSG00000186716
	ENSMUSG00000009681
	P11274
	Q6PAJ1
	NM_004327; NM_021574
	NM_001081412
	NP_004318; NP_067585
	NP_001074881
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Protein regije klasterske prelomne tačke'" (BCR), znan I kao antigen bubrežnog karcinoma NY-REN-26 jest protein koji je kod ljudi kodiran genom BCR sa hromosoma 22. BCR je jedan od dva gena u kompleksu BCR-ABL, koji je povezan sa filadelfija hromosomom. Za ovaj gen su pronađene dvije varijante transkripta koje kodiraju različite izoforme.

Aminokiselinska sekvenca[uredi | uredi izvor]

Dužina polipeptidnog lanca je 1.271 aminokiselina, a molekulska težina 142.819 Da.

C: Cistein

D: Asparaginska kiselina

E: Glutaminska kiselina

F: Fenilalanin

G: Glicin

H: Histidin

I: Izoleucin

K: Lizin

L: Leucin

M: Metionin

N: Asparagin

P: Prolin

Q: Glutamin

R: Arginin

S: Serin

T: Treonin

V: Valin

W: Triptofan

Y: Tirozin

10	20	30	40	50
MVDPVGFAEA	WKAQFPDSEP	PRMELRSVGD	IEQELERCKA	SIRRLEQEVN
QERFRMIYLQ	TLLAKEKKSY	DRQRWGFRRA	AQAPDGASEP	RASASRPQPA
PADGADPPPA	EEPEARPDGE	GSPGKARPGT	ARRPGAAASG	ERDDRGPPAS
VAALRSNFER	IRKGHGQPGA	DAEKPFYVNV	EFHHERGLVK	VNDKEVSDRI
SSLGSQAMQM	ERKKSQHGAG	SSVGDASRPP	YRGRSSESSC	GVDGDYEDAE
LNPRFLKDNL	IDANGGSRPP	WPPLEYQPYQ	SIYVGGMMEG	EGKGPLLRSQ
STSEQEKRLT	WPRRSYSPRS	FEDCGGGYTP	DCSSNENLTS	SEEDFSSGQS
SRVSPSPTTY	RMFRDKSRSP	SQNSQQSFDS	SSPPTPQCHK	RHRHCPVVVS
EATIVGVRKT	GQIWPNDGEG	AFHGDADGSF	GTPPGYGCAA	DRAEEQRRHQ
DGLPYIDDSP	SSSPHLSSKG	RGSRDALVSG	ALESTKASEL	DLEKGLEMRK
WVLSGILASE	ETYLSHLEAL	LLPMKPLKAA	ATTSQPVLTS	QQIETIFFKV
PELYEIHKEF	YDGLFPRVQQ	WSHQQRVGDL	FQKLASQLGV	YRAFVDNYGV
AMEMAEKCCQ	ANAQFAEISE	NLRARSNKDA	KDPTTKNSLE	TLLYKPVDRV
TRSTLVLHDL	LKHTPASHPD	HPLLQDALRI	SQNFLSSINE	EITPRRQSMT
VKKGEHRQLL	KDSFMVELVE	GARKLRHVFL	FTDLLLCTKL	KKQSGGKTQQ
YDCKWYIPLT	DLSFQMVDEL	EAVPNIPLVP	DEELDALKIK	ISQIKNDIQR
EKRANKGSKA	TERLKKKLSE	QESLLLLMSP	SMAFRVHSRN	GKSYTFLISS
DYERAEWREN	IREQQKKCFR	SFSLTSVELQ	MLTNSCVKLQ	TVHSIPLTIN
KEDDESPGLY	GFLNVIVHSA	TGFKQSSNLY	CTLEVDSFGY	FVNKAKTRVY
RDTAEPNWNE	EFEIELEGSQ	TLRILCYEKC	YNKTKIPKED	GESTDRLMGK
GQVQLDPQAL	QDRDWQRTVI	AMNGIEVKLS	VKFNSREFSL	KRMPSRKQTG
VFGVKIAVVT	KRERSKVPYI	VRQCVEEIER	RGMEEVGIYR	VSGVATDIQA
LKAAFDVNNK	DVSVMMSEMD	VNAIAGTLKL	YFRELPEPLF	TDEFYPNFAE
GIALSDPVAK	ESCMLNLLLS	LPEANLLTFL	FLLDHLKRVA	EKEAVNKMSL
HNLATVFGPT	LLRPSEKESK	LPANPSQPIT	MTDSWSLEVM	SQVQVLLYFL
QLEAIPAPDS	KRQSILFSTE	V

Struktura[uredi | uredi izvor]

Domen oligomerizacije onkoproteina BCR-ABL koji se nalazi na N-terminalu BCR je od suštinskog značaja za onkogenost fuzijskog protein BCR-ABL. Domen oligomerizacije onkoproteina BCR-ABL sastoji se od kratkog N-terminalnog alfa-heliksa (alfa-1), fleksibilne petlje i dugog C-terminalnog heliksa (alfa-2). Oni zajedno formiraju strukturu u obliku slova N, sa petljom koja omogućava da dva heliksa zauzmu paralelnu orijentaciju. Monomerni domeni povezuju se u dimer, m antiparalelne upredene zavojnice između alfa-heliksa -2 i domena zamjena dva alfa-1 heliksa, pri čemu se jedan alfa-1 heliks okreće unazad i nabije na alfa-2 heliks iz drugog monomera. Dva dimera se zatim povezuju u tetramer.^[5]

Funkcija[uredi | uredi izvor]

Iako je BCR-ABL fuzijski protein proučavan bezbroj puta, funkcija normalnog BCR genskog proizvoda još uvijek nije jasna. Protein ima aktivnost serin/treonin kinaza i faktora izmjene gvanin-nukleotida za porodicu Rho GTPaza, uključujući RhoA.^[6]^[7]

Klinički značaj[uredi | uredi izvor]

Recipročna translokacija između hromosoma 22 i 9 proizvodi filadelfija hromosom], koji se često nalazi kod pacijenata sa hroničnom mijelogenom leukemijom. Prelomna tačka hromosoma 22 za ovu translokaciju nalazi se unutar gena "BCR". Translokacija proizvodi fuzijski protein koji je kodiran sekvencom iz "BCR" i "ABL", gena na tački prekida hromosoma 9.^[8]

Interakcije[uredi | uredi izvor]

Pokazalo se da BCR protein u interakciji sa:

Abl gen,^[9]^[10]^[11]
CD117,^[12]
CRKL^[13]^[14]^[15]^[16]
FES,^[17]^[18]
Grb2,^[9]^[13]^[14]^[18]^[19]^[20]
GRB10,^[13]
HCK,^[21]^[22]
MLLT4,^[23]
PXN,^[24]^[25]
PIK3CG,^[13]^[24]^[26]
PTPN6,^[27]
PTPRT(PTPrho)^[28]
SOS1,^[9]^[18] i
XPB.^[29]

Također pogledajte[uredi | uredi izvor]

Gen Abl

Reference[uredi | uredi izvor]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000186716 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000009681 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Zhao X, Ghaffari S, Lodish H, Malashkevich VN, Kim PS (February 2002). "Structure of the Bcr-Abl oncoprotein oligomerization domain". Nat. Struct. Biol. 9 (2): 117–20. doi:10.1038/nsb747. PMID 11780146. S2CID 17453012.
^ Dubash, Adi D.; Koetsier, Jennifer L.; Amargo, Evangeline V.; Najor, Nicole A.; Harmon, Robert M.; Green, Kathleen J. (2013-08-19). "The GEF Bcr activates RhoA/MAL signaling to promote keratinocyte differentiation via desmoglein-1". The Journal of Cell Biology. 202 (4): 653–666. doi:10.1083/jcb.201304133. ISSN 0021-9525. PMC 3747303. PMID 23940119.
^ "Entrez Gene: Breakpoint cluster region".
^ "Entrez Gene: BCR breakpoint cluster region".
^ ^a ^b ^c Puil L, Liu J, Gish G, Mbamalu G, Bowtell D, Pelicci PG, Arlinghaus R, Pawson T (February 1994). "Bcr-Abl oncoproteins bind directly to activators of the Ras signalling pathway". EMBO J. 13 (4): 764–73. doi:10.1002/j.1460-2075.1994.tb06319.x. PMC 394874. PMID 8112292.
^ Ling X, Ma G, Sun T, Liu J, Arlinghaus RB (January 2003). "Bcr and Abl interaction: oncogenic activation of c-Abl by sequestering Bcr". Cancer Res. 63 (2): 298–303. PMID 12543778.
^ Pendergast AM, Muller AJ, Havlik MH, Maru Y, Witte ON (July 1991). "BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner". Cell. 66 (1): 161–71. doi:10.1016/0092-8674(91)90148-R. PMID 1712671. S2CID 9933891.
^ Hallek M, Danhauser-Riedl S, Herbst R, Warmuth M, Winkler A, Kolb HJ, Druker B, Griffin JD, Emmerich B, Ullrich A (July 1996). "Interaction of the receptor tyrosine kinase p145c-kit with the p210bcr/abl kinase in myeloid cells". Br. J. Haematol. 94 (1): 5–16. doi:10.1046/j.1365-2141.1996.6102053.x. PMID 8757502. S2CID 30033345.
^ ^a ^b ^c ^d Bai RY, Jahn T, Schrem S, Munzert G, Weidner KM, Wang JY, Duyster J (August 1998). "The SH2-containing adapter protein GRB10 interacts with BCR-ABL". Oncogene. 17 (8): 941–8. doi:10.1038/sj.onc.1202024. PMID 9747873. S2CID 20866214.
^ ^a ^b Million RP, Harakawa N, Roumiantsev S, Varticovski L, Van Etten RA (June 2004). "A direct binding site for Grb2 contributes to transformation and leukemogenesis by the Tel-Abl (ETV6-Abl) tyrosine kinase". Mol. Cell. Biol. 24 (11): 4685–95. doi:10.1128/MCB.24.11.4685-4695.2004. PMC 416425. PMID 15143164.
^ Heaney C, Kolibaba K, Bhat A, Oda T, Ohno S, Fanning S, Druker BJ (January 1997). "Direct binding of CRKL to BCR-ABL is not required for BCR-ABL transformation". Blood. 89 (1): 297–306. doi:10.1182/blood.V89.1.297. PMID 8978305.
^ Kolibaba KS, Bhat A, Heaney C, Oda T, Druker BJ (March 1999). "CRKL binding to BCR-ABL and BCR-ABL transformation". Leuk. Lymphoma. 33 (1–2): 119–26. doi:10.3109/10428199909093732. PMID 10194128.
^ Lionberger JM, Smithgall TE (February 2000). "The c-Fes protein-tyrosine kinase suppresses cytokine-independent outgrowth of myeloid leukemia cells induced by Bcr-Abl". Cancer Res. 60 (4): 1097–103. PMID 10706130.
^ ^a ^b ^c Maru Y, Peters KL, Afar DE, Shibuya M, Witte ON, Smithgall TE (February 1995). "Tyrosine phosphorylation of BCR by FPS/FES protein-tyrosine kinases induces association of BCR with GRB-2/SOS". Mol. Cell. Biol. 15 (2): 835–42. doi:10.1128/MCB.15.2.835. PMC 231961. PMID 7529874.
^ Million RP, Van Etten RA (July 2000). "The Grb2 binding site is required for the induction of chronic myeloid leukemia-like disease in mice by the Bcr/Abl tyrosine kinase". Blood. 96 (2): 664–70. doi:10.1182/blood.V96.2.664. PMID 10887132.
^ Ma G, Lu D, Wu Y, Liu J, Arlinghaus RB (May 1997). "Bcr phosphorylated on tyrosine 177 binds Grb2". Oncogene. 14 (19): 2367–72. doi:10.1038/sj.onc.1201053. PMID 9178913. S2CID 9249479.
^ Stanglmaier M, Warmuth M, Kleinlein I, Reis S, Hallek M (February 2003). "The interaction of the Bcr-Abl tyrosine kinase with the Src kinase Hck is mediated by multiple binding domains". Leukemia. 17 (2): 283–9. doi:10.1038/sj.leu.2402778. PMID 12592324. S2CID 8695384.
^ Lionberger JM, Wilson MB, Smithgall TE (June 2000). "Transformation of myeloid leukemia cells to cytokine independence by Bcr-Abl is suppressed by kinase-defective Hck". J. Biol. Chem. 275 (24): 18581–5. doi:10.1074/jbc.C000126200. PMID 10849448.
^ Radziwill G, Erdmann RA, Margelisch U, Moelling K (July 2003). "The Bcr kinase downregulates Ras signaling by phosphorylating AF-6 and binding to its PDZ domain". Mol. Cell. Biol. 23 (13): 4663–72. doi:10.1128/MCB.23.13.4663-4672.2003. PMC 164848. PMID 12808105.
^ ^a ^b Salgia R, Sattler M, Pisick E, Li JL, Griffin JD (February 1996). "p210BCR/ABL induces formation of complexes containing focal adhesion proteins and the protooncogene product p120c-Cbl". Exp. Hematol. 24 (2): 310–3. PMID 8641358.
^ Salgia R, Li JL, Lo SH, Brunkhorst B, Kansas GS, Sobhany ES, Sun Y, Pisick E, Hallek M, Ernst T (March 1995). "Molecular cloning of human paxillin, a focal adhesion protein phosphorylated by P210BCR/ABL". J. Biol. Chem. 270 (10): 5039–47. doi:10.1074/jbc.270.10.5039. PMID 7534286.
^ Skorski T, Kanakaraj P, Nieborowska-Skorska M, Ratajczak MZ, Wen SC, Zon G, Gewirtz AM, Perussia B, Calabretta B (July 1995). "Phosphatidylinositol-3 kinase activity is regulated by BCR/ABL and is required for the growth of Philadelphia chromosome-positive cells". Blood. 86 (2): 726–36. doi:10.1182/blood.V86.2.726.bloodjournal862726. PMID 7606002.
^ Liedtke M, Pandey P, Kumar S, Kharbanda S, Kufe D (October 1998). "Regulation of Bcr-Abl-induced SAP kinase activity and transformation by the SHPTP1 protein tyrosine phosphatase". Oncogene. 17 (15): 1889–92. doi:10.1038/sj.onc.1202117. PMID 9788431. S2CID 42228230.
^ Park AR, Oh D, Lim SH, Choi J, Moon J, Yu DY, Park SG, Heisterkamp N, Kim E, Myung PK, Lee JR (2012). "Regulation of dendritic arborization by BCR Rac1 GTPase-activating protein, a substrate of PTPRT". J. Cell Sci. 125 (Pt 19): 4518–31. doi:10.1242/jcs.105502. PMID 22767509. S2CID 22422544.
^ Takeda N, Shibuya M, Maru Y (January 1999). "The BCR-ABL oncoprotein potentially interacts with the xeroderma pigmentosum group B protein". Proc. Natl. Acad. Sci. U.S.A. 96 (1): 203–7. Bibcode:1999PNAS...96..203T. doi:10.1073/pnas.96.1.203. PMC 15117. PMID 9874796.

Dopunska literatura[uredi | uredi izvor]

Wang L, Seale J, Woodcock BE, Clark RE (2002). "e19a2-positive chronic myeloid leukaemia with BCR exon e16-deleted transcripts". Leukemia. 16 (8): 1562–3. doi:10.1038/sj.leu.2402600. PMID 12145699. S2CID 24651759.

Vanjski linkovi[uredi | uredi izvor]

BCR protein, human na US National Library of Medicine Medical Subject Headings (MeSH)
Lokacija ljudskog genoma BCR i stranica sa detaljima o genu BCR u UCSC Genome Browseru.
P11274

Ovaj članak uključuje tekst iz javnog domena Pfam i InterPro: IPR015123

Kategorijka:Protein kinaze

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000186716 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000009681 - Ensembl, maj 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid11780146-5] Zhao X, Ghaffari S, Lodish H, Malashkevich VN, Kim PS (February 2002). "Structure of the Bcr-Abl oncoprotein oligomerization domain". Nat. Struct. Biol. 9 (2): 117–20. doi:10.1038/nsb747. PMID 11780146. S2CID 17453012.

[6] Dubash, Adi D.; Koetsier, Jennifer L.; Amargo, Evangeline V.; Najor, Nicole A.; Harmon, Robert M.; Green, Kathleen J. (2013-08-19). "The GEF Bcr activates RhoA/MAL signaling to promote keratinocyte differentiation via desmoglein-1". The Journal of Cell Biology. 202 (4): 653–666. doi:10.1083/jcb.201304133. ISSN 0021-9525. PMC 3747303. PMID 23940119.

[entrez-7] "Entrez Gene: Breakpoint cluster region".

[8] "Entrez Gene: BCR breakpoint cluster region".

[pmid8112292-9] Puil L, Liu J, Gish G, Mbamalu G, Bowtell D, Pelicci PG, Arlinghaus R, Pawson T (February 1994). "Bcr-Abl oncoproteins bind directly to activators of the Ras signalling pathway". EMBO J. 13 (4): 764–73. doi:10.1002/j.1460-2075.1994.tb06319.x. PMC 394874. PMID 8112292.

[pmid12543778-10] Ling X, Ma G, Sun T, Liu J, Arlinghaus RB (January 2003). "Bcr and Abl interaction: oncogenic activation of c-Abl by sequestering Bcr". Cancer Res. 63 (2): 298–303. PMID 12543778.

[pmid1712671-11] Pendergast AM, Muller AJ, Havlik MH, Maru Y, Witte ON (July 1991). "BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner". Cell. 66 (1): 161–71. doi:10.1016/0092-8674(91)90148-R. PMID 1712671. S2CID 9933891.

[pmid8757502-12] Hallek M, Danhauser-Riedl S, Herbst R, Warmuth M, Winkler A, Kolb HJ, Druker B, Griffin JD, Emmerich B, Ullrich A (July 1996). "Interaction of the receptor tyrosine kinase p145c-kit with the p210bcr/abl kinase in myeloid cells". Br. J. Haematol. 94 (1): 5–16. doi:10.1046/j.1365-2141.1996.6102053.x. PMID 8757502. S2CID 30033345.

[pmid9747873-13] Bai RY, Jahn T, Schrem S, Munzert G, Weidner KM, Wang JY, Duyster J (August 1998). "The SH2-containing adapter protein GRB10 interacts with BCR-ABL". Oncogene. 17 (8): 941–8. doi:10.1038/sj.onc.1202024. PMID 9747873. S2CID 20866214.

[pmid15143164-14] Million RP, Harakawa N, Roumiantsev S, Varticovski L, Van Etten RA (June 2004). "A direct binding site for Grb2 contributes to transformation and leukemogenesis by the Tel-Abl (ETV6-Abl) tyrosine kinase". Mol. Cell. Biol. 24 (11): 4685–95. doi:10.1128/MCB.24.11.4685-4695.2004. PMC 416425. PMID 15143164.

[pmid8978305-15] Heaney C, Kolibaba K, Bhat A, Oda T, Ohno S, Fanning S, Druker BJ (January 1997). "Direct binding of CRKL to BCR-ABL is not required for BCR-ABL transformation". Blood. 89 (1): 297–306. doi:10.1182/blood.V89.1.297. PMID 8978305.

[pmid10194128-16] Kolibaba KS, Bhat A, Heaney C, Oda T, Druker BJ (March 1999). "CRKL binding to BCR-ABL and BCR-ABL transformation". Leuk. Lymphoma. 33 (1–2): 119–26. doi:10.3109/10428199909093732. PMID 10194128.

[pmid10706130-17] Lionberger JM, Smithgall TE (February 2000). "The c-Fes protein-tyrosine kinase suppresses cytokine-independent outgrowth of myeloid leukemia cells induced by Bcr-Abl". Cancer Res. 60 (4): 1097–103. PMID 10706130.

[pmid7529874-18] Maru Y, Peters KL, Afar DE, Shibuya M, Witte ON, Smithgall TE (February 1995). "Tyrosine phosphorylation of BCR by FPS/FES protein-tyrosine kinases induces association of BCR with GRB-2/SOS". Mol. Cell. Biol. 15 (2): 835–42. doi:10.1128/MCB.15.2.835. PMC 231961. PMID 7529874.

[pmid10887132-19] Million RP, Van Etten RA (July 2000). "The Grb2 binding site is required for the induction of chronic myeloid leukemia-like disease in mice by the Bcr/Abl tyrosine kinase". Blood. 96 (2): 664–70. doi:10.1182/blood.V96.2.664. PMID 10887132.

[pmid9178913-20] Ma G, Lu D, Wu Y, Liu J, Arlinghaus RB (May 1997). "Bcr phosphorylated on tyrosine 177 binds Grb2". Oncogene. 14 (19): 2367–72. doi:10.1038/sj.onc.1201053. PMID 9178913. S2CID 9249479.

[pmid12592324-21] Stanglmaier M, Warmuth M, Kleinlein I, Reis S, Hallek M (February 2003). "The interaction of the Bcr-Abl tyrosine kinase with the Src kinase Hck is mediated by multiple binding domains". Leukemia. 17 (2): 283–9. doi:10.1038/sj.leu.2402778. PMID 12592324. S2CID 8695384.

[pmid10849448-22] Lionberger JM, Wilson MB, Smithgall TE (June 2000). "Transformation of myeloid leukemia cells to cytokine independence by Bcr-Abl is suppressed by kinase-defective Hck". J. Biol. Chem. 275 (24): 18581–5. doi:10.1074/jbc.C000126200. PMID 10849448.

[pmid12808105-23] Radziwill G, Erdmann RA, Margelisch U, Moelling K (July 2003). "The Bcr kinase downregulates Ras signaling by phosphorylating AF-6 and binding to its PDZ domain". Mol. Cell. Biol. 23 (13): 4663–72. doi:10.1128/MCB.23.13.4663-4672.2003. PMC 164848. PMID 12808105.

[pmid8641358-24] Salgia R, Sattler M, Pisick E, Li JL, Griffin JD (February 1996). "p210BCR/ABL induces formation of complexes containing focal adhesion proteins and the protooncogene product p120c-Cbl". Exp. Hematol. 24 (2): 310–3. PMID 8641358.

[pmid7534286-25] Salgia R, Li JL, Lo SH, Brunkhorst B, Kansas GS, Sobhany ES, Sun Y, Pisick E, Hallek M, Ernst T (March 1995). "Molecular cloning of human paxillin, a focal adhesion protein phosphorylated by P210BCR/ABL". J. Biol. Chem. 270 (10): 5039–47. doi:10.1074/jbc.270.10.5039. PMID 7534286.

[pmid7606002-26] Skorski T, Kanakaraj P, Nieborowska-Skorska M, Ratajczak MZ, Wen SC, Zon G, Gewirtz AM, Perussia B, Calabretta B (July 1995). "Phosphatidylinositol-3 kinase activity is regulated by BCR/ABL and is required for the growth of Philadelphia chromosome-positive cells". Blood. 86 (2): 726–36. doi:10.1182/blood.V86.2.726.bloodjournal862726. PMID 7606002.

[pmid9788431-27] Liedtke M, Pandey P, Kumar S, Kharbanda S, Kufe D (October 1998). "Regulation of Bcr-Abl-induced SAP kinase activity and transformation by the SHPTP1 protein tyrosine phosphatase". Oncogene. 17 (15): 1889–92. doi:10.1038/sj.onc.1202117. PMID 9788431. S2CID 42228230.

[pmid22767509-28] Park AR, Oh D, Lim SH, Choi J, Moon J, Yu DY, Park SG, Heisterkamp N, Kim E, Myung PK, Lee JR (2012). "Regulation of dendritic arborization by BCR Rac1 GTPase-activating protein, a substrate of PTPRT". J. Cell Sci. 125 (Pt 19): 4518–31. doi:10.1242/jcs.105502. PMID 22767509. S2CID 22422544.

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