RAC1

RAC1
"rac1"이 여기로 리디렉션된다.Ratchet & Clank 시리즈의 첫 번째 게임은 Ratchet & Clank를 참조하십시오.
RAC1
Protein RAC1 PDB 1ds6.png
사용 가능한 구조물
PDB직교 검색: PDBe RCSB
식별자
별칭RAC1, MIG5, Rac-1, TC-25, p21-Rac1, ras 관련 C3 보툴리눔 독소 기질 1(rho 제품군, 소형 GTP 결합 단백질 Rac1) Rac 제품군 소 GTPase 1, MRD48
외부 IDOMIM: 602048 MGI: 97845 HomoloGene: 69035 GeneCard: RAC1
직교체
종인간마우스
엔트레스

5879

19353

앙상블

ENSG00000136238

ENSMUSG00000001847

유니프로트

P63000

P63001

RefSeq(mRNA)

NM_198829
NM_006908
NM_018890

NM_009007
NM_001347530

RefSeq(단백질)

NP_008839
NP_061485

NP_001334459
NP_033033

위치(UCSC)Chr 7: 6.37 – 6.4MbChr 5: 143.49 – 143.51Mb
PubMed 검색[3][4]
위키다타
인간 보기/편집마우스 보기/편집

Rac1은 Ras 관련 C3 보툴리눔 톡신 기질 1로도 알려져 있으며, 인간 세포에서 발견되는 단백질이다.그것은 RAC1 유전자에 의해 암호화된다.[5][6]이 유전자는 Rac1 단백질의 여러 가지 다른 분할 버전을 만들 수 있는데, 이것은 다른 기능을 수행하는 것으로 보인다.[7]

함수

Rac1은 G단백질(더 구체적으로는 GTPase)을 신호하는 작은 (~21kDa)이며, GTPases의 Rho 계열의 Rac 하위 계열의 일원이다.이 슈퍼 패밀리의 구성원들은 글루코스 섭취에 대한 글루트4[8][9] 변환 제어, 세포 성장, 세포 골격계 재구성, 항균 세포독성,[10] 단백질 키나제 활성화 등 다양한 셀룰러 이벤트를 규제하는 것으로 보인다.[11]

Rac1은 세포 주기, 세포-세포 접착, 운동성(액틴 네트워크를 통한) 및 상피 분화(피피질 줄기세포 유지에 필요한 것으로 제안됨)를 포함한 많은 세포 과정들의 플립방성 조절기다.

암에서의 역할

Rac과 Rho 단백질의 다른 하위 제품군과 함께, 그들은 세포 운동성과 세포 성장에 특히 중요한 규제 역할을 한다.Rac1은 유비쿼터스 조직표현을 가지고 있으며, 라멜리포디아의 형성에 의해 세포 운동성을 촉진한다.[12]암세포가 성장하여 국소 및 원거리 조직을 침범하기 위해서는 세포운동성 규제완화가 암세포의 침입과 전이에서 두드러진 사건 중 하나이다.[13]쥐에서 구성성 있는 활성 Rac1 V12의 과도한 압착은 표현적으로 카포시의 육종과 구별할 수 없는 종양을 유발했다.[14]Rac1의 기능상 돌연변이를 활성화하거나 활성화하는 것은 NEDD9과 DOK3 단백질 복합체가 지원하는 중피형 세포 운동을 촉진하는 데 적극적인 역할을 하는 것으로 보인다.[15]이러한 비정상적인 세포 운동성으로 인해 상피 중피 전이(EMT)가 발생할 수 있는데, 이는 종양 전이뿐만 아니라 약물 내성 종양 재발에 대한 추진 메커니즘이다.[16][17]

포도당 운반의 역할

Rac1은 지방 조직과 골격근과 같은 인슐린 민감 조직에서 상당한 양으로 표현된다.여기서 Rac1은 GLUT4 vesicle을 세포내 구획에서 플라즈마 막으로 운반하는 포도당의 변환을 규제했다.[9][18][19]인슐린에 반응하여, 이것은 혈당이 혈당을 낮추기 위해 세포 안으로 들어갈 수 있게 한다.비만과 제2형 당뇨병의 경우 골격근에 Rac1 신호가 기능장애가 있어 Rac1이 병의 진행에 기여함을 시사한다.Rac1 단백질은 운동과[8][20] 근육 스트레칭으로[21] 활성화된 골격근의 포도당 섭취에도 필요하다.

임상적 유의성

Rac1에서 돌연변이를 활성화시키는 것은 최근 흑색종과[22][23][24] 비소세포 폐암과 관련된 대규모 유전체 연구에서 발견되었다.[25]그 결과, Rac1은 이러한 많은 질병의 치료 대상으로 여겨지고 있다.[26]

최근의 몇몇 연구들은 또한 인간의 유방암뿐만 아니라 전이성 흑색종과 간암에서 Rac1 활동을 약리학적으로 억제함으로써 종양의 성장을 억제하는 표적 요법을 이용했다.[27][28][29]예를 들어 Rac1 의존 경로 억제 결과 종양세포 표현형식이 역전되어 Rac1이 트라스투주맙 내성 유방암의 예측표지자 치료목표로 제시되었다.[28]그러나 포도당 운반에 있어 Rac1의 역할을 감안할 때 Rac1을 억제하는 약물은 포도당 동점선상에 잠재적으로 해로울 수 있다.

지배적인 음수 또는 구성성 활성 세균라인 RAC1 돌연변이는 정신 지체 유형 48로 함께 그룹화된 다양한 표현형을 유발한다.[30]대부분의 돌연변이는 소두증을 유발하는 반면 어떤 특정한 변화는 대두증을 유발하는 것으로 보인다.

상호작용

RAC1은 다음과 상호 작용하는 것으로 나타났다.

참조

  1. ^ a b c GRCh38: 앙상블 릴리스 89: ENSG00000136238 - 앙상블, 2017년 5월
  2. ^ a b c GRCm38: 앙상블 릴리스 89: ENSMUSG00000001847 - 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. ^ Didsbury J, Weber RF, Bokoch GM, Evans T, Snyderman R (Oct 1989). "rac, a novel ras-related family of proteins that are botulinum toxin substrates". The Journal of Biological Chemistry. 264 (28): 16378–82. doi:10.1016/S0021-9258(19)84716-6. PMID 2674130.
  6. ^ Jordan P, Brazåo R, Boavida MG, Gespach C, Chastre E (Nov 1999). "Cloning of a novel human Rac1b splice variant with increased expression in colorectal tumors". Oncogene. 18 (48): 6835–9. doi:10.1038/sj.onc.1203233. PMID 10597294.
  7. ^ Zhou C, Licciulli S, Avila JL, Cho M, Troutman S, Jiang P, Kossenkov AV, Showe LC, Liu Q, Vachani A, Albelda SM, Kissil JL (Feb 2013). "The Rac1 splice form Rac1b promotes K-ras-induced lung tumorigenesis". Oncogene. 32 (7): 903–9. doi:10.1038/onc.2012.99. PMC 3384754. PMID 22430205.
  8. ^ a b Sylow, Lykke; Nielsen, Ida L.; Kleinert, Maximilian; Møller, Lisbeth L. V.; Ploug, Thorkil; Schjerling, Peter; Bilan, Philip J.; Klip, Amira; Jensen, Thomas E. (2016-04-09). "Rac1 governs exercise-stimulated glucose uptake in skeletal muscle through regulation of GLUT4 translocation in mice". The Journal of Physiology. 594 (17): 4997–5008. doi:10.1113/JP272039. ISSN 1469-7793. PMC 5009787. PMID 27061726.
  9. ^ a b Ueda S, Kitazawa S, Ishida K, Nishikawa Y, Matsui M, Matsumoto H, Aoki T, Nozaki S, Takeda T, Tamori Y, Aiba A, Kahn CR, Kataoka T, Satoh T (Jul 2010). "Crucial role of the small GTPase Rac1 in insulin-stimulated translocation of glucose transporter 4 to the mouse skeletal muscle sarcolemma". FASEB Journal. 24 (7): 2254–61. doi:10.1096/fj.09-137380. PMC 4183928. PMID 20203090.
  10. ^ Xiang RF (Mar 2016). "Ras-related C3 Botulinum Toxin Substrate (Rac) and Src Family Kinases (SFK) Are Proximal and Essential for Phosphatidylinositol 3-Kinase (PI3K) Activation in Natural Killer (NK) Cell-mediated Direct Cytotoxicity against Cryptococcus neoformans". J Biol Chem. 291 (13): 6912–22. doi:10.1074/jbc.M115.681544. PMC 4807276. PMID 26867574.
  11. ^ Ridley AJ (Oct 2006). "Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking". Trends in Cell Biology. 16 (10): 522–9. doi:10.1016/j.tcb.2006.08.006. PMID 16949823.
  12. ^ Parri M, Chiarugi P (2010). "Rac and Rho GTPases in cancer cell motility control". Cell Communication and Signaling. 8 (23): 23. doi:10.1186/1478-811x-8-23. PMC 2941746. PMID 20822528.
  13. ^ Hanahan D, Weinberg RA (Mar 2011). "Hallmarks of cancer: the next generation". Cell. 144 (5): 646–74. doi:10.1016/j.cell.2011.02.013. PMID 21376230.
  14. ^ Ma, Qi; Cavallin, Lucas E.; Yan, Bin; Zhu, Shoukang; Duran, Elda Margarita; Wang, Huili; Hale, Laura P.; Dong, Chunming; Cesarman, Ethel (2009-05-26). "Antitumorigenesis of antioxidants in a transgenic Rac1 model of Kaposi's sarcoma". Proceedings of the National Academy of Sciences. 106 (21): 8683–8688. doi:10.1073/pnas.0812688106. ISSN 0027-8424. PMC 2679580. PMID 19429708.
  15. ^ Sanz-Moreno V, Gadea G, Ahn J, Paterson H, Marra P, Pinner S, Sahai E, Marshall CJ (Oct 2008). "Rac activation and inactivation control plasticity of tumor cell movement". Cell. 135 (3): 510–23. doi:10.1016/j.cell.2008.09.043. PMID 18984162. S2CID 5745856.
  16. ^ Stallings-Mann ML, Waldmann J, Zhang Y, Miller E, Gauthier ML, Visscher DW, et al. (Jul 11, 2012). "Matrix metalloproteinase induction of Rac1b, a key effector of lung cancer progression". Science Translational Medicine. 4 (142): 510–523. doi:10.1126/scitranslmed.3004062. PMC 3733503. PMID 22786680.
  17. ^ Yang WH, Lan HY, Huang CH, Tai SK, Tzeng CH, Kao SY, Wu KJ, Hung MC, Yang MH (Apr 2012). "RAC1 activation mediates Twist1-induced cancer cell migration". Nature Cell Biology. 14 (4): 366–74. doi:10.1038/ncb2455. PMID 22407364. S2CID 4755216.
  18. ^ Sylow L, Kleinert M, Pehmøller C, Prats C, Chiu TT, Klip A, Richter EA, Jensen TE (Feb 2014). "Akt and Rac1 signaling are jointly required for insulin-stimulated glucose uptake in skeletal muscle and downregulated in insulin resistance". Cellular Signalling. 26 (2): 323–31. doi:10.1016/j.cellsig.2013.11.007. PMID 24216610.
  19. ^ Sylow L, Jensen TE, Kleinert M, Højlund K, Kiens B, Wojtaszewski J, Prats C, Schjerling P, Richter EA (Jun 2013). "Rac1 signaling is required for insulin-stimulated glucose uptake and is dysregulated in insulin-resistant murine and human skeletal muscle". Diabetes. 62 (6): 1865–75. doi:10.2337/db12-1148. PMC 3661612. PMID 23423567.
  20. ^ Sylow L, Jensen TE, Kleinert M, Mouatt JR, Maarbjerg SJ, Jeppesen J, Prats C, Chiu TT, Boguslavsky S, Klip A, Schjerling P, Richter EA (Apr 2013). "Rac1 is a novel regulator of contraction-stimulated glucose uptake in skeletal muscle". Diabetes. 62 (4): 1139–51. doi:10.2337/db12-0491. PMC 3609592. PMID 23274900.
  21. ^ Sylow L, Møller LL, Kleinert M, Richter EA, Jensen TE (Feb 2015). "Stretch-stimulated glucose transport in skeletal muscle is regulated by Rac1". The Journal of Physiology. 593 (3): 645–56. doi:10.1113/jphysiol.2014.284281. PMC 4324711. PMID 25416624.
  22. ^ Hodis E, Watson IR, Kryukov GV, Arold ST, Imielinski M, Theurillat JP, Nickerson E, Auclair D, Li L, Place C, Dicara D, Ramos AH, Lawrence MS, Cibulskis K, Sivachenko A, Voet D, Saksena G, Stransky N, Onofrio RC, Winckler W, Ardlie K, Wagle N, Wargo J, Chong K, Morton DL, Stemke-Hale K, Chen G, Noble M, Meyerson M, Ladbury JE, Davies MA, Gershenwald JE, Wagner SN, Hoon DS, Schadendorf D, Lander ES, Gabriel SB, Getz G, Garraway LA, Chin L (Jul 2012). "A landscape of driver mutations in melanoma". Cell. 150 (2): 251–63. doi:10.1016/j.cell.2012.06.024. PMC 3600117. PMID 22817889.
  23. ^ Krauthammer M, Kong Y, Ha BH, Evans P, Bacchiocchi A, McCusker JP, Cheng E, Davis MJ, Goh G, Choi M, Ariyan S, Narayan D, Dutton-Regester K, Capatana A, Holman EC, Bosenberg M, Sznol M, Kluger HM, Brash DE, Stern DF, Materin MA, Lo RS, Mane S, Ma S, Kidd KK, Hayward NK, Lifton RP, Schlessinger J, Boggon TJ, Halaban R (Sep 2012). "Exome sequencing identifies recurrent somatic RAC1 mutations in melanoma". Nature Genetics. 44 (9): 1006–14. doi:10.1038/ng.2359. PMC 3432702. PMID 22842228.
  24. ^ Bauer NN, Chen YW, Samant RS, Shevde LA, Fodstad O (Nov 2007). "Rac1 activity regulates proliferation of aggressive metastatic melanoma". Experimental Cell Research. 313 (18): 3832–9. doi:10.1016/j.yexcr.2007.08.017. PMID 17904119.
  25. ^ Stallings-Mann ML, Waldmann J, Zhang Y, Miller E, Gauthier ML, Visscher DW, Downey GP, Radisky ES, Fields AP, Radisky DC (Jul 2012). "Matrix metalloproteinase induction of Rac1b, a key effector of lung cancer progression". Science Translational Medicine. 4 (142): 142ra95. doi:10.1126/scitranslmed.3004062. PMC 3733503. PMID 22786680.
  26. ^ McAllister SS (Jul 2012). "Got a light? Illuminating lung cancer". Science Translational Medicine. 4 (142): 142fs22. doi:10.1126/scitranslmed.3004446. PMID 22786678. S2CID 12093516.
  27. ^ Chen QY, Xu LQ, Jiao DM, Yao QH, Wang YY, Hu HZ, et al. (Nov 2011). "Silencing of Rac1 modifies lung cancer cell migration, invasion and actin cytoskeleton rearrangements and enhances chemosensitivity to antitumor drugs". International Journal of Molecular Medicine. 28 (5): 769–776. doi:10.3892/ijmm.2011.775. PMID 21837360.
  28. ^ a b Dokmanovic M, Hirsch DS, Shen Y, Wu WJ (Jun 2009). "Rac1 contributes to trastuzumab resistance of breast cancer cells: Rac1 as a potential therapeutic target for the treatment of trastuzumab-resistant breast cancer". Molecular Cancer Therapeutics. 8 (6): 1557–69. doi:10.1158/1535-7163.mct-09-0140. PMID 19509242.
  29. ^ Liu S, Yu M, He Y, Xiao L, Wang F, Song C, Sun S, Ling C, Xu Z (Jun 2008). "Melittin prevents liver cancer cell metastasis through inhibition of the Rac1-dependent pathway". Hepatology. 47 (6): 1964–73. doi:10.1002/hep.22240. PMID 18506888. S2CID 21106205.
  30. ^ Reijnders, Margot R.F.; Ansor, Nurhuda M.; Kousi, Maria; Yue, Wyatt W.; Tan, Perciliz L.; Clarkson, Katie; Clayton-Smith, Jill; Corning, Ken; Jones, Julie R.; Lam, Wayne W.K.; Mancini, Grazia M.S.; Marcelis, Carlo; Mohammed, Shehla; Pfundt, Rolph; Roifman, Maian; Cohn, Ronald; Chitayat, David; Millard, Tom H.; Katsanis, Nicholas; Brunner, Han G.; Banka, Siddharth (September 2017). "RAC1 Missense Mutations in Developmental Disorders with Diverse Phenotypes". The American Journal of Human Genetics. 101 (3): 466–477. doi:10.1016/j.ajhg.2017.08.007. PMC 5591022. PMID 28886345.
  31. ^ a b Shin OH, Exton JH (Aug 2001). "Differential binding of arfaptin 2/POR1 to ADP-ribosylation factors and Rac1". Biochemical and Biophysical Research Communications. 285 (5): 1267–73. doi:10.1006/bbrc.2001.5330. PMID 11478794.
  32. ^ Van Aelst L, Joneson T, Bar-Sagi D (Aug 1996). "Identification of a novel Rac1-interacting protein involved in membrane ruffling". The EMBO Journal. 15 (15): 3778–86. doi:10.1002/j.1460-2075.1996.tb00751.x. PMC 452058. PMID 8670882.
  33. ^ Tarricone C, Xiao B, Justin N, Walker PA, Rittinger K, Gamblin SJ, Smerdon SJ (May 2001). "The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways". Nature. 411 (6834): 215–9. doi:10.1038/35075620. PMID 11346801. S2CID 4324211.
  34. ^ Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
  35. ^ Grizot S, Fauré J, Fieschi F, Vignais PV, Dagher MC, Pebay-Peyroula E (Aug 2001). "Crystal structure of the Rac1-RhoGDI complex involved in nadph oxidase activation". Biochemistry. 40 (34): 10007–13. doi:10.1021/bi010288k. PMID 11513578.
  36. ^ Lian LY, Barsukov I, Golovanov AP, Hawkins DI, Badii R, Sze KH, Keep NH, Bokoch GM, Roberts GC (Jan 2000). "Mapping the binding site for the GTP-binding protein Rac-1 on its inhibitor RhoGDI-1". Structure. 8 (1): 47–55. doi:10.1016/S0969-2126(00)00080-0. PMID 10673424.
  37. ^ Gorvel JP, Chang TC, Boretto J, Azuma T, Chavrier P (Jan 1998). "Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity". FEBS Letters. 422 (2): 269–73. doi:10.1016/S0014-5793(98)00020-9. PMID 9490022. S2CID 10817327.
  38. ^ Di-Poï N, Fauré J, Grizot S, Molnár G, Pick E, Dagher MC (Aug 2001). "Mechanism of NADPH oxidase activation by the Rac/Rho-GDI complex". Biochemistry. 40 (34): 10014–22. doi:10.1021/bi010289c. PMID 11513579.
  39. ^ Fauré J, Dagher MC (May 2001). "Interactions between Rho GTPases and Rho GDP dissociation inhibitor (Rho-GDI)". Biochimie. 83 (5): 409–14. doi:10.1016/S0300-9084(01)01263-9. PMID 11368848.
  40. ^ Miki H, Yamaguchi H, Suetsugu S, Takenawa T (Dec 2000). "IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling". Nature. 408 (6813): 732–5. doi:10.1038/35047107. PMID 11130076. S2CID 4426046.
  41. ^ Westendorf JJ (Dec 2001). "The formin/diaphanous-related protein, FHOS, interacts with Rac1 and activates transcription from the serum response element". The Journal of Biological Chemistry. 276 (49): 46453–9. doi:10.1074/jbc.M105162200. PMID 11590143.
  42. ^ Yayoshi-Yamamoto S, Taniuchi I, Watanabe T (Sep 2000). "FRL, a novel formin-related protein, binds to Rac and regulates cell motility and survival of macrophages". Molecular and Cellular Biology. 20 (18): 6872–81. doi:10.1128/MCB.20.18.6872-6881.2000. PMC 86228. PMID 10958683.
  43. ^ a b Zhang B, Chernoff J, Zheng Y (Apr 1998). "Interaction of Rac1 with GTPase-activating proteins and putative effectors. A comparison with Cdc42 and RhoA". The Journal of Biological Chemistry. 273 (15): 8776–82. doi:10.1074/jbc.273.15.8776. PMID 9535855.
  44. ^ Kuroda S, Fukata M, Kobayashi K, Nakafuku M, Nomura N, Iwamatsu A, Kaibuchi K (Sep 1996). "Identification of IQGAP as a putative target for the small GTPases, Cdc42 and Rac1". The Journal of Biological Chemistry. 271 (38): 23363–7. doi:10.1074/jbc.271.38.23363. PMID 8798539.
  45. ^ Fukata M, Watanabe T, Noritake J, Nakagawa M, Yamaga M, Kuroda S, Matsuura Y, Iwamatsu A, Perez F, Kaibuchi K (Jun 2002). "Rac1 and Cdc42 capture microtubules through IQGAP1 and CLIP-170". Cell. 109 (7): 873–85. doi:10.1016/S0092-8674(02)00800-0. PMID 12110184. S2CID 15158637.
  46. ^ Hart MJ, Callow MG, Souza B, Polakis P (Jun 1996). "IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for cdc42Hs". The EMBO Journal. 15 (12): 2997–3005. doi:10.1002/j.1460-2075.1996.tb00663.x. PMC 450241. PMID 8670801.
  47. ^ Brill S, Li S, Lyman CW, Church DM, Wasmuth JJ, Weissbach L, Bernards A, Snijders AJ (Sep 1996). "The Ras GTPase-activating-protein-related human protein IQGAP2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases". Molecular and Cellular Biology. 16 (9): 4869–78. doi:10.1128/mcb.16.9.4869. PMC 231489. PMID 8756646.
  48. ^ Jefferies C, Bowie A, Brady G, Cooke EL, Li X, O'Neill LA (Jul 2001). "Transactivation by the p65 subunit of NF-kappaB in response to interleukin-1 (IL-1) involves MyD88, IL-1 receptor-associated kinase 1, TRAF-6, and Rac1" (PDF). Molecular and Cellular Biology. 21 (14): 4544–52. doi:10.1128/MCB.21.14.4544-4552.2001. PMC 87113. PMID 11416133.
  49. ^ Shimizu M, Wang W, Walch ET, Dunne PW, Epstein HF (Jun 2000). "Rac-1 and Raf-1 kinases, components of distinct signaling pathways, activate myotonic dystrophy protein kinase". FEBS Letters. 475 (3): 273–7. doi:10.1016/S0014-5793(00)01692-6. PMID 10869570. S2CID 46238883.
  50. ^ Kitamura Y, Kitamura T, Sakaue H, Maeda T, Ueno H, Nishio S, Ohno S, Osada S, Sakaue M, Ogawa W, Kasuga M (Mar 1997). "Interaction of Nck-associated protein 1 with activated GTP-binding protein Rac". The Biochemical Journal. 322 (3): 873–8. doi:10.1042/bj3220873. PMC 1218269. PMID 9148763.
  51. ^ Katoh H, Negishi M (Jul 2003). "RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo". Nature. 424 (6947): 461–4. doi:10.1038/nature01817. PMID 12879077. S2CID 4411133.
  52. ^ Seoh ML, Ng CH, Yong J, Lim L, Leung T (Mar 2003). "ArhGAP15, a novel human RacGAP protein with GTPase binding property". FEBS Letters. 539 (1–3): 131–7. doi:10.1016/S0014-5793(03)00213-8. PMID 12650940. S2CID 27574424.
  53. ^ a b Noda Y, Takeya R, Ohno S, Naito S, Ito T, Sumimoto H (Feb 2001). "Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C". Genes to Cells. 6 (2): 107–19. doi:10.1046/j.1365-2443.2001.00404.x. PMID 11260256. S2CID 8789941.
  54. ^ Qiu RG, Abo A, Steven Martin G (Jun 2000). "A human homolog of the C. elegans polarity determinant Par-6 links Rac and Cdc42 to PKCzeta signaling and cell transformation". Current Biology. 10 (12): 697–707. doi:10.1016/S0960-9822(00)00535-2. PMID 10873802. S2CID 14825707.
  55. ^ Zhao C, Ma H, Bossy-Wetzel E, Lipton SA, Zhang Z, Feng GS (Sep 2003). "GC-GAP, a Rho family GTPase-activating protein that interacts with signaling adapters Gab1 and Gab2". The Journal of Biological Chemistry. 278 (36): 34641–53. doi:10.1074/jbc.M304594200. PMID 12819203.
  56. ^ Moon SY, Zang H, Zheng Y (Feb 2003). "Characterization of a brain-specific Rho GTPase-activating protein, p200RhoGAP". The Journal of Biological Chemistry. 278 (6): 4151–9. doi:10.1074/jbc.M207789200. PMID 12454018.
  57. ^ Simon AR, Vikis HG, Stewart S, Fanburg BL, Cochran BH, Guan KL (Oct 2000). "Regulation of STAT3 by direct binding to the Rac1 GTPase". Science. 290 (5489): 144–7. doi:10.1126/science.290.5489.144. PMID 11021801.
  58. ^ Worthylake DK, Rossman KL, Sondek J (Dec 2000). "Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1". Nature. 408 (6813): 682–8. doi:10.1038/35047014. PMID 11130063. S2CID 4429919.
  59. ^ Gao Y, Xing J, Streuli M, Leto TL, Zheng Y (Dec 2001). "Trp(56) of rac1 specifies interaction with a subset of guanine nucleotide exchange factors". The Journal of Biological Chemistry. 276 (50): 47530–41. doi:10.1074/jbc.M108865200. PMID 11595749.

추가 읽기

외부 링크