야누스키나제2길

Janus kinase 2
JAK2
Protein JAK2 PDB 2b7a.png
사용 가능한 구조물
PDB직교 검색: PDBe RCSB
식별자
별칭JAC2, JTK10, TCYT3, Janus kinase 2, MAX2
외부 IDOMIM: 147796 MGI: 96629 호몰로진: 21033 GeneCard: JAK2
직교체
인간마우스
엔트레스
앙상블
유니프로트
RefSeq(mRNA)

NM_001048177
NM_008413

RefSeq(단백질)

NP_001041642
NP_032439

위치(UCSC)Cr 9: 4.98 – 5.13MbCr 19: 29.23 – 29.29Mb
PubMed 검색[3][4]
위키다타
인간 보기/편집마우스 보기/편집

Janus kinase 2(일반적으로 JAK2)는 비수용체 tyrosine kinase이다.It is a member of the Janus kinase family and has been implicated in signaling by members of the type II cytokine receptor family (e.g. interferon receptors), the GM-CSF receptor family (IL-3R, IL-5R and GM-CSF-R), the gp130 receptor family (e.g., IL-6R), and the single chain receptors (e.g. Epo-R, Tpo-R, GH-R, PRL-R).[5][6]

janus kinase 2와 다른 JAK kinases의 구별되는 특징은 Src homology binding domain(SH2/SH3)의 부족과 최대 7개의 JAK homology domain(JH1-JH7)이다.그럼에도 불구하고 터미널 JH 도메인은 tyrosine kinase 도메인에 대한 높은 수준의 호몰로지를 유지한다.흥미로운 점은 이러한 카복시-단자 JH 도메인 중 하나만 전체 키나제 함수(JH1)를 유지하며, 이전에 키나제 기능이 없다고 생각되어 유사키나제 도메인이라고 불리던 다른 도메인(JH2)은 그 이후 JH1 도메인의 10%에 불과하지만 촉매적으로 활성 상태인 것으로 밝혀졌다.[7][8]

Jak2의 상실은 쥐의 배아날 12일에 의해 치명적이다.[9]

JAK2 정형외과들[10] 완전한 게놈 데이터를 이용할 수 있는 모든 포유류에서 확인되었다.

임상적 유의성

TEL(ETV6)과 PCM1 유전자를 가진 JAK2 유전자 융합이 백혈병을 앓고 있는 환자들, 특히 이 질병의 집단적 어소니아필리아 형태에서 발견되었다.[11][12][13]

JAK2의 돌연변이는 다른 골수종 장애뿐만 아니라 다낭성 베라, 필수 혈소판 테마니아, 골수성 신경증, 골수성 장애와 관련이 있다.[14]617 위치에서 발린이 페닐알라닌으로 변화한 이 돌연변이(V617F)는 조혈세포에리트로포이에틴트롬보포에틴과 같은 성장요인에 더 민감하게 만드는 것으로 보인다. 이러한 성장요인의 수용체는 신호전달을 위해 JAK2를 필요로 하기 때문이다.JAK2-STAT5의 억제제인 AZD1480은 1차 및 CRPC에서 활동이 있는 것으로 지적되었다.[15] Jak2 돌연변이는, 증명할 수 있을 때, 다시테마니아 베라를 진단하는 방법 중 하나이다.[16]

상호작용

Janus kinase 2는 다음과 상호작용하는 것으로 나타났다.

JAC2를 통한 프로락틴 신호는 STAT5RUSH 전사 인자에 따라 달라진다.[60]

참고 항목

참조

  1. ^ a b c GRCh38: 앙상블 릴리스 89: ENSG000096968 - 앙상블, 2017년 5월
  2. ^ a b c GRCm38: 앙상블 릴리스 89: ENSMUSG000024789 - 앙상블, 2017년 5월
  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.
  5. ^ Bole-Feysot C, Goffin V, Edery M, Binart N, Kelly PA (June 1998). "Prolactin (PRL) and its receptor: actions, signal transduction pathways and phenotypes observed in PRL receptor knockout mice". Endocrine Reviews. 19 (3): 225–68. doi:10.1210/edrv.19.3.0334. PMID 9626554.
  6. ^ Brooks AJ, Dai W, O'Mara ML, Abankwa D, Chhabra Y, Pelekanos RA, et al. (2014). "Mechanism of activation of protein kinase JAK2 by the growth hormone receptor". Science. 344 (6185): 1249783. doi:10.1126/science.1249783. PMID 24833397. S2CID 27946074.
  7. ^ Morgan KJ, Gilliland DG (2008). "A role for JAK2 mutations in myeloproliferative diseases". Annual Review of Medicine. 59 (1): 213–22. doi:10.1146/annurev.med.59.061506.154159. PMID 17919086.
  8. ^ Ungureanu D, Wu J, Pekkala T, Niranjan Y, Young C, Jensen ON, Xu CF, Neubert TA, Skoda RC, Hubbard SR, Silvennoinen O (August 2011). "The pseudokinase domain of JAK2 is a dual-specificity protein kinase that negatively regulates cytokine signaling". Nature Structural & Molecular Biology. 18 (9): 971–976. doi:10.1038/nsmb.2099. PMC 4504201. PMID 21841788.
  9. ^ Neubauer H, Cumano A, Müller M, Wu H, Huffstadt U, Pfeffer K (May 1998). "Jak2 deficiency defines an essential developmental checkpoint in definitive hematopoiesis". Cell. 93 (3): 397–409. doi:10.1016/S0092-8674(00)81168-X. PMID 9590174. S2CID 11375232.
  10. ^ "OrthoMaM phylogenetic marker: JAK2 coding sequence".[영구적 데드링크]
  11. ^ Lacronique V, Boureux A, Valle VD, Poirel H, Quang CT, Mauchauffé M, Berthou C, Lessard M, Berger R, Ghysdael J, Bernard OA (November 1997). "A TEL-JAK2 fusion protein with constitutive kinase activity in human leukemia". Science. 278 (5341): 1309–12. Bibcode:1997Sci...278.1309L. doi:10.1126/science.278.5341.1309. PMID 9360930.
  12. ^ Reiter A, Walz C, Watmore A, Schoch C, Blau I, Schlegelberger B, Berger U, Telford N, Aruliah S, Yin JA, Vanstraelen D, Barker HF, Taylor PC, O'Driscoll A, Benedetti F, Rudolph C, Kolb HJ, Hochhaus A, Hehlmann R, Chase A, Cross NC (April 2005). "The t(8;9)(p22;p24) is a recurrent abnormality in chronic and acute leukemia that fuses PCM1 to JAK2". Cancer Research. 65 (7): 2662–7. doi:10.1158/0008-5472.CAN-04-4263. PMID 15805263.
  13. ^ Reiter A, Gotlib J (2017). "Myeloid neoplasms with eosinophilia". Blood. 129 (6): 704–714. doi:10.1182/blood-2016-10-695973. PMID 28028030.
  14. ^ Kralovics R, Passamonti F, Buser AS, Teo SS, Tiedt R, Passweg JR, Tichelli A, Cazzola M, Skoda RC (April 2005). "A gain-of-function mutation of JAK2 in myeloproliferative disorders". The New England Journal of Medicine. 352 (17): 1779–90. doi:10.1056/NEJMoa051113. PMID 15858187.
  15. ^ Gu L, Liao Z, Hoang DT, Dagvadorj A, Gupta S, Blackmon S, Ellsworth E, Talati P, Leiby B, Zinda M, Lallas CD, Trabulsi EJ, McCue P, Gomella L, Huszar D, Nevalainen MT (October 2013). "Pharmacologic inhibition of Jak2-Stat5 signaling By Jak2 inhibitor AZD1480 potently suppresses growth of both primary and castrate-resistant prostate cancer". Clinical Cancer Research. 19 (20): 5658–74. doi:10.1158/1078-0432.CCR-13-0422. PMC 6021137. PMID 23942095.
  16. ^ Scott LM (August 2011). "The JAK2 exon 12 mutations: a comprehensive review". American Journal of Hematology. 86 (8): 668–76. doi:10.1002/ajh.22063. PMID 21674578. S2CID 2905512.
  17. ^ Sarkar S, Pollack BP, Lin KT, Kotenko SV, Cook JR, Lewis A, Pestka S (December 2001). "hTid-1, a human DnaJ protein, modulates the interferon signaling pathway". The Journal of Biological Chemistry. 276 (52): 49034–42. doi:10.1074/jbc.M103683200. PMID 11679576.
  18. ^ Olayioye MA, Beuvink I, Horsch K, Daly JM, Hynes NE (June 1999). "ErbB receptor-induced activation of stat transcription factors is mediated by Src tyrosine kinases". The Journal of Biological Chemistry. 274 (24): 17209–18. doi:10.1074/jbc.274.24.17209. PMID 10358079.
  19. ^ Huang LJ, Constantinescu SN, Lodish HF (December 2001). "The N-terminal domain of Janus kinase 2 is required for Golgi processing and cell surface expression of erythropoietin receptor". Molecular Cell. 8 (6): 1327–38. doi:10.1016/S1097-2765(01)00401-4. PMID 11779507.
  20. ^ Witthuhn BA, Quelle FW, Silvennoinen O, Yi T, Tang B, Miura O, Ihle JN (July 1993). "JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin". Cell. 74 (2): 227–36. doi:10.1016/0092-8674(93)90414-L. PMID 8343951. S2CID 37503350.
  21. ^ Sayeski PP, Ali MS, Safavi A, Lyles M, Kim SO, Frank SJ, Bernstein KE (November 1999). "A catalytically active Jak2 is required for the angiotensin II-dependent activation of Fyn". The Journal of Biological Chemistry. 274 (46): 33131–42. doi:10.1074/jbc.274.46.33131. PMID 10551884.
  22. ^ Chauhan D, Kharbanda SM, Ogata A, Urashima M, Frank D, Malik N, Kufe DW, Anderson KC (December 1995). "Oncostatin M induces association of Grb2 with Janus kinase JAK2 in multiple myeloma cells". The Journal of Experimental Medicine. 182 (6): 1801–6. doi:10.1084/jem.182.6.1801. PMC 2192257. PMID 7500025.
  23. ^ Giorgetti-Peraldi S, Peyrade F, Baron V, Van Obberghen E (December 1995). "Involvement of Janus kinases in the insulin signaling pathway". European Journal of Biochemistry. 234 (2): 656–60. doi:10.1111/j.1432-1033.1995.656_b.x. PMID 8536716.
  24. ^ Frank SJ, Yi W, Zhao Y, Goldsmith JF, Gilliland G, Jiang J, Sakai I, Kraft AS (June 1995). "Regions of the JAK2 tyrosine kinase required for coupling to the growth hormone receptor". The Journal of Biological Chemistry. 270 (24): 14776–85. doi:10.1074/jbc.270.24.14776. PMID 7540178.
  25. ^ VanderKuur JA, Wang X, Zhang L, Campbell GS, Allevato G, Billestrup N, Norstedt G, Carter-Su C (August 1994). "Domains of the growth hormone receptor required for association and activation of JAK2 tyrosine kinase". The Journal of Biological Chemistry. 269 (34): 21709–17. doi:10.1016/S0021-9258(17)31863-X. PMID 8063815.
  26. ^ Hellgren G, Jansson JO, Carlsson LM, Carlsson B (June 1999). "The growth hormone receptor associates with Jak1, Jak2 and Tyk2 in human liver". Growth Hormone & IGF Research. 9 (3): 212–8. doi:10.1054/ghir.1999.0111. PMID 10502458.
  27. ^ Gual P, Baron V, Lequoy V, Van Obberghen E (March 1998). "Interaction of Janus kinases JAK-1 and JAK-2 with the insulin receptor and the insulin-like growth factor-1 receptor". Endocrinology. 139 (3): 884–93. doi:10.1210/endo.139.3.5829. PMID 9492017.
  28. ^ Kawazoe Y, Naka T, Fujimoto M, Kohzaki H, Morita Y, Narazaki M, Okumura K, Saitoh H, Nakagawa R, Uchiyama Y, Akira S, Kishimoto T (January 2001). "Signal transducer and activator of transcription (STAT)-induced STAT inhibitor 1 (SSI-1)/suppressor of cytokine signaling 1 (SOCS1) inhibits insulin signal transduction pathway through modulating insulin receptor substrate 1 (IRS-1) phosphorylation". The Journal of Experimental Medicine. 193 (2): 263–9. doi:10.1084/jem.193.2.263. PMC 2193341. PMID 11208867.
  29. ^ Yamamoto K, Shibata F, Miura O, Kamiyama R, Hirosawa S, Miyasaka N (April 1999). "Physical interaction between interleukin-12 receptor beta 2 subunit and Jak2 tyrosine kinase: Jak2 associates with cytoplasmic membrane-proximal region of interleukin-12 receptor beta 2 via amino-terminus". Biochemical and Biophysical Research Communications. 257 (2): 400–4. doi:10.1006/bbrc.1999.0479. PMID 10198225.
  30. ^ Ogata N, Kouro T, Yamada A, Koike M, Hanai N, Ishikawa T, Takatsu K (April 1998). "JAK2 and JAK1 constitutively associate with an interleukin-5 (IL-5) receptor alpha and betac subunit, respectively, and are activated upon IL-5 stimulation". Blood. 91 (7): 2264–71. doi:10.1182/blood.V91.7.2264. PMID 9516124.
  31. ^ a b c Fuhrer DK, Yang YC (July 1996). "Complex formation of JAK2 with PP2A, P13K, and Yes in response to the hematopoietic cytokine interleukin-11". Biochemical and Biophysical Research Communications. 224 (2): 289–96. doi:10.1006/bbrc.1996.1023. PMID 8702385.
  32. ^ Zhu T, Goh EL, Lobie PE (April 1998). "Growth hormone stimulates the tyrosine phosphorylation and association of p125 focal adhesion kinase (FAK) with JAK2. Fak is not required for stat-mediated transcription". The Journal of Biological Chemistry. 273 (17): 10682–9. doi:10.1074/jbc.273.17.10682. PMID 9553131.
  33. ^ Ryu H, Lee JH, Kim KS, Jeong SM, Kim PH, Chung HT (August 2000). "Regulation of neutrophil adhesion by pituitary growth hormone accompanies tyrosine phosphorylation of Jak2, p125FAK, and paxillin". Journal of Immunology. 165 (4): 2116–23. doi:10.4049/jimmunol.165.4.2116. PMID 10925297.
  34. ^ Yin T, Shen R, Feng GS, Yang YC (January 1997). "Molecular characterization of specific interactions between SHP-2 phosphatase and JAK tyrosine kinases". The Journal of Biological Chemistry. 272 (2): 1032–7. doi:10.1074/jbc.272.2.1032. PMID 8995399.
  35. ^ Tauchi T, Damen JE, Toyama K, Feng GS, Broxmeyer HE, Krystal G (June 1996). "Tyrosine 425 within the activated erythropoietin receptor binds Syp, reduces the erythropoietin required for Syp tyrosine phosphorylation, and promotes mitogenesis". Blood. 87 (11): 4495–501. doi:10.1182/blood.V87.11.4495.bloodjournal87114495. PMID 8639815.
  36. ^ Maegawa H, Kashiwagi A, Fujita T, Ugi S, Hasegawa M, Obata T, Nishio Y, Kojima H, Hidaka H, Kikkawa R (November 1996). "SHPTP2 serves adapter protein linking between Janus kinase 2 and insulin receptor substrates". Biochemical and Biophysical Research Communications. 228 (1): 122–7. doi:10.1006/bbrc.1996.1626. PMID 8912646.
  37. ^ Jiao H, Berrada K, Yang W, Tabrizi M, Platanias LC, Yi T (December 1996). "Direct association with and dephosphorylation of Jak2 kinase by the SH2-domain-containing protein tyrosine phosphatase SHP-1". Molecular and Cellular Biology. 16 (12): 6985–92. doi:10.1128/mcb.16.12.6985. PMC 231702. PMID 8943354.
  38. ^ Wu DW, Stark KC, Dunnington D, Dillon SB, Yi T, Jones C, Pelus LM (February 2000). "SH2-Containing protein tyrosine phosphatase-1 (SHP-1) association with Jak2 in UT-7/Epo cells". Blood Cells, Molecules & Diseases. 26 (1): 15–24. doi:10.1006/bcmd.2000.0273. PMID 10772872.
  39. ^ Pollack BP, Kotenko SV, He W, Izotova LS, Barnoski BL, Pestka S (October 1999). "The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity". The Journal of Biological Chemistry. 274 (44): 31531–42. doi:10.1074/jbc.274.44.31531. PMID 10531356.
  40. ^ Rui L, Mathews LS, Hotta K, Gustafson TA, Carter-Su C (November 1997). "Identification of SH2-Bbeta as a substrate of the tyrosine kinase JAK2 involved in growth hormone signaling". Molecular and Cellular Biology. 17 (11): 6633–44. doi:10.1128/mcb.17.11.6633. PMC 232517. PMID 9343427.
  41. ^ Xie S, Lin H, Sun T, Arlinghaus RB (October 2002). "Jak2 is involved in c-Myc induction by Bcr-Abl". Oncogene. 21 (47): 7137–46. doi:10.1038/sj.onc.1205942. PMID 12370803.
  42. ^ VanderKuur J, Allevato G, Billestrup N, Norstedt G, Carter-Su C (March 1995). "Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SHC association with Grb2". The Journal of Biological Chemistry. 270 (13): 7587–93. doi:10.1074/jbc.270.13.7587. PMID 7535773.
  43. ^ Giordano V, De Falco G, Chiari R, Quinto I, Pelicci PG, Bartholomew L, Delmastro P, Gadina M, Scala G (May 1997). "Shc mediates IL-6 signaling by interacting with gp130 and Jak2 kinase". Journal of Immunology. 158 (9): 4097–103. PMID 9126968.
  44. ^ Sasaki A, Yasukawa H, Shouda T, Kitamura T, Dikic I, Yoshimura A (September 2000). "CIS3/SOCS-3 suppresses erythropoietin (EPO) signaling by binding the EPO receptor and JAK2". The Journal of Biological Chemistry. 275 (38): 29338–47. doi:10.1074/jbc.M003456200. PMID 10882725.
  45. ^ Sasaki A, Yasukawa H, Suzuki A, Kamizono S, Syoda T, Kinjyo I, Sasaki M, Johnston JA, Yoshimura A (June 1999). "Cytokine-inducible SH2 protein-3 (CIS3/SOCS3) inhibits Janus tyrosine kinase by binding through the N-terminal kinase inhibitory region as well as SH2 domain". Genes to Cells. 4 (6): 339–51. doi:10.1046/j.1365-2443.1999.00263.x. PMID 10421843. S2CID 24871585.
  46. ^ a b Masuhara M, Sakamoto H, Matsumoto A, Suzuki R, Yasukawa H, Mitsui K, Wakioka T, Tanimura S, Sasaki A, Misawa H, Yokouchi M, Ohtsubo M, Yoshimura A (October 1997). "Cloning and characterization of novel CIS family genes". Biochemical and Biophysical Research Communications. 239 (2): 439–46. doi:10.1006/bbrc.1997.7484. PMID 9344848.
  47. ^ a b Barahmand-Pour F, Meinke A, Groner B, Decker T (May 1998). "Jak2-Stat5 interactions analyzed in yeast". The Journal of Biological Chemistry. 273 (20): 12567–75. doi:10.1074/jbc.273.20.12567. PMID 9575217.
  48. ^ a b Fujitani Y, Hibi M, Fukada T, Takahashi-Tezuka M, Yoshida H, Yamaguchi T, Sugiyama K, Yamanaka Y, Nakajima K, Hirano T (February 1997). "An alternative pathway for STAT activation that is mediated by the direct interaction between JAK and STAT". Oncogene. 14 (7): 751–61. doi:10.1038/sj.onc.1200907. PMID 9047382.
  49. ^ Takeshita T, Arita T, Higuchi M, Asao H, Endo K, Kuroda H, Tanaka N, Murata K, Ishii N, Sugamura K (April 1997). "STAM, signal transducing adaptor molecule, is associated with Janus kinases and involved in signaling for cell growth and c-myc induction". Immunity. 6 (4): 449–57. doi:10.1016/S1074-7613(00)80288-5. PMID 9133424.
  50. ^ Yasukawa H, Misawa H, Sakamoto H, Masuhara M, Sasaki A, Wakioka T, Ohtsuka S, Imaizumi T, Matsuda T, Ihle JN, Yoshimura A (March 1999). "The JAK-binding protein JAB inhibits Janus tyrosine kinase activity through binding in the activation loop". The EMBO Journal. 18 (5): 1309–20. doi:10.1093/emboj/18.5.1309. PMC 1171221. PMID 10064597.
  51. ^ Dif F, Saunier E, Demeneix B, Kelly PA, Edery M (December 2001). "Cytokine-inducible SH2-containing protein suppresses PRL signaling by binding the PRL receptor". Endocrinology. 142 (12): 5286–93. doi:10.1210/endo.142.12.8549. PMID 11713228.
  52. ^ Endo TA, Masuhara M, Yokouchi M, Suzuki R, Sakamoto H, Mitsui K, Matsumoto A, Tanimura S, Ohtsubo M, Misawa H, Miyazaki T, Leonor N, Taniguchi T, Fujita T, Kanakura Y, Komiya S, Yoshimura A (June 1997). "A new protein containing an SH2 domain that inhibits JAK kinases". Nature. 387 (6636): 921–4. Bibcode:1997Natur.387..921E. doi:10.1038/43213. PMID 9202126. S2CID 4347361.
  53. ^ Pezet A, Favre H, Kelly PA, Edery M (August 1999). "Inhibition and restoration of prolactin signal transduction by suppressors of cytokine signaling". The Journal of Biological Chemistry. 274 (35): 24497–502. doi:10.1074/jbc.274.35.24497. PMID 10455112.
  54. ^ Ungureanu D, Saharinen P, Junttila I, Hilton DJ, Silvennoinen O (May 2002). "Regulation of Jak2 through the ubiquitin-proteasome pathway involves phosphorylation of Jak2 on Y1007 and interaction with SOCS-1". Molecular and Cellular Biology. 22 (10): 3316–26. doi:10.1128/MCB.22.10.3316-3326.2002. PMC 133778. PMID 11971965.
  55. ^ Takahashi-Tezuka M, Hibi M, Fujitani Y, Fukada T, Yamaguchi T, Hirano T (May 1997). "Tec tyrosine kinase links the cytokine receptors to PI-3 kinase probably through JAK". Oncogene. 14 (19): 2273–82. doi:10.1038/sj.onc.1201071. PMID 9178903.
  56. ^ Yamashita Y, Watanabe S, Miyazato A, Ohya Ki, Ikeda U, Shimada K, Komatsu N, Hatake K, Miura Y, Ozawa K, Mano H (March 1998). "Tec and Jak2 kinases cooperate to mediate cytokine-driven activation of c-fos transcription". Blood. 91 (5): 1496–507. doi:10.1182/blood.V91.5.1496. PMID 9473212.
  57. ^ Guo D, Dunbar JD, Yang CH, Pfeffer LM, Donner DB (March 1998). "Induction of Jak/STAT signaling by activation of the type 1 TNF receptor". Journal of Immunology. 160 (6): 2742–50. PMID 9510175.
  58. ^ Shigematsu H, Iwasaki H, Otsuka T, Ohno Y, Arima F, Niho Y (May 1997). "Role of the vav proto-oncogene product (Vav) in erythropoietin-mediated cell proliferation and phosphatidylinositol 3-kinase activity". The Journal of Biological Chemistry. 272 (22): 14334–40. doi:10.1074/jbc.272.22.14334. PMID 9162069.
  59. ^ Matsuguchi T, Inhorn RC, Carlesso N, Xu G, Druker B, Griffin JD (January 1995). "Tyrosine phosphorylation of p95Vav in myeloid cells is regulated by GM-CSF, IL-3 and steel factor and is constitutively increased by p210BCR/ABL". EMBO J. 14 (2): 257–65. doi:10.1002/j.1460-2075.1995.tb06999.x. PMC 398079. PMID 7530656.
  60. ^ Helmer RA, Panchoo M, Dertien JS, Bhakta SM, Hewetson A, Chilton BS (August 2010). "Prolactin-induced Jak2 phosphorylation of RUSH: a key element in Jak/RUSH signaling". Molecular and Cellular Endocrinology. 325 (1–2): 143–9. doi:10.1016/j.mce.2010.05.010. PMC 2902710. PMID 20562009.

추가 읽기

외부 링크