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{{Infobox_gene}}
{{PBB_Controls
'''PAK3''' (p21-activated kinase 2, beta-PAK) is one of three members of Group I PAK family of evolutionary conserved [[serine/threonine kinases]].<ref>{{cite journal | vauthors = Knaus UG, Morris S, Dong HJ, Chernoff J, Bokoch GM | title = Regulation of human leukocyte p21-activated kinases through G protein--coupled receptors | journal = Science | volume = 269 | issue = 5221 | pages = 221–3 | date = July 1995 | pmid = 7618083 | doi = 10.1126/science.7618083 }}</ref><ref>{{cite journal | vauthors = Manser E, Chong C, Zhao ZS, Leung T, Michael G, Hall C, Lim L | title = Molecular cloning of a new member of the p21-Cdc42/Rac-activated kinase (PAK) family | journal = The Journal of Biological Chemistry | volume = 270 | issue = 42 | pages = 25070–8 | date = October 1995 | pmid = 7559638 | doi = 10.1074/jbc.270.42.25070 }}</ref><ref>{{cite journal | vauthors = Kumar A, Molli PR, Pakala SB, Bui Nguyen TM, Rayala SK, Kumar R | title = PAK thread from amoeba to mammals | journal = Journal of Cellular Biochemistry | volume = 107 | issue = 4 | pages = 579–85 | date = July 2009 | pmid = 19350548 | pmc = 2718766 | doi = 10.1002/jcb.22159 }}</ref> PAK3 is preferentially expressed in neuronal cells <ref name="RA">{{cite journal | vauthors = Bagrodia S, Taylor SJ, Creasy CL, Chernoff J, Cerione RA | title = Identification of a mouse p21Cdc42/Rac activated kinase | journal = The Journal of Biological Chemistry | volume = 270 | issue = 39 | pages = 22731–7 | date = September 1995 | pmid = 7559398 | doi = 10.1074/jbc.270.39.22731 }}</ref><ref name="DM">{{cite journal | vauthors = Burbelo PD, Kozak CA, Finegold AA, Hall A, Pirone DM | title = Cloning, central nervous system expression and chromosomal mapping of the mouse PAK-1 and PAK-3 genes | journal = Gene | volume = 232 | issue = 2 | pages = 209–15 | date = May 1999 | pmid = 10352232 | doi = 10.1016/s0378-1119(99)00110-9 }}</ref> and involved in [[synapse]] formation and plasticity and [[Intellectual disability|mental retardation]].<ref name="D">{{cite journal | vauthors = Boda B, Alberi S, Nikonenko I, Node-Langlois R, Jourdain P, Moosmayer M, Parisi-Jourdain L, Muller D | title = The mental retardation protein PAK3 contributes to synapse formation and plasticity in hippocampus | journal = The Journal of Neuroscience | volume = 24 | issue = 48 | pages = 10816–25 | date = December 2004 | pmid = 15574732 | doi = 10.1523/jneurosci.2931-04.2004 }}</ref><ref name="CA">{{cite journal | vauthors = Allen KM, Gleeson JG, Bagrodia S, Partington MW, MacMillan JC, Cerione RA, Mulley JC, Walsh CA | title = PAK3 mutation in nonsyndromic X-linked mental retardation | journal = Nature Genetics | volume = 20 | issue = 1 | pages = 25–30 | date = September 1998 | pmid = 9731525 | doi = 10.1038/1675 }}</ref>
| update_page = yes
 
| require_manual_inspection = no
== Discovery ==
| update_protein_box = yes
PAK3 was initially cloned from a murine fibroblast [[cDNA library]] and from a murine embryo cDNA library.<ref name="RA" /><ref name="DM" /> Like other group I PAKs, PAK3 is stimulated by activated [[CDC42|Cdc42]] and [[RAC1|Rac1]].
| update_summary = yes
 
| update_citations = yes
== Gene and spliced variants ==
}}
The human PAK3 gene, the longest group I family member, is 283-kb long. The PAK3 gene is composed of 22 [[Exon|exons]] of which 6 exons are for 5’-UTR and generates 13 alternative spliced [[Transcription (biology)|transcripts]]. Among PAK3 transcripts, 11 transcripts are for coding proteins ranging from 181- to 580-amino acids long, while remaining two transcripts are [[Non-coding RNA|non-coding RNAs]].<ref>{{cite journal | vauthors = Kreis P, Rousseau V, Thévenot E, Combeau G, Barnier JV | title = The four mammalian splice variants encoded by the p21-activated kinase 3 gene have different biological properties | journal = Journal of Neurochemistry | volume = 106 | issue = 3 | pages = 1184–97 | date = August 2008 | pmid = 18507705 | doi = 10.1111/j.1471-4159.2008.05474.x }}</ref> The murine PAK3 gene contains 10 transcripts, coding six proteins from 544 amino acids and 559 amino acids long, and four smaller polypeptides from 23 to 366 amino acids.
 
== Protein domains ==
Similar to [[PAK1]], PAK2 contains a p21-binding domain (PBD) and an auto-inhibitory domain (AID) and exists in an inactive conformation.<ref>{{Cite book | vauthors = Kumar R, Li DQ | title = PAKs in Human Cancer Progression: From Inception to Cancer Therapeutic to Future Oncobiology | journal = Advances in Cancer Research | volume = 130 | pages = 137–209 | date = 2016 | pmid = 27037753 | doi = 10.1016/bs.acr.2016.01.002 | isbn = 9780128047897 }}</ref>


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Activators and inhibitors ==
{{GNF_Protein_box
PAK3 activity is stimulated by Dbl, Cdc42 and Cool-2,<ref>{{cite journal | vauthors = Bagrodia S, Bailey D, Lenard Z, Hart M, Guan JL, Premont RT, Taylor SJ, Cerione RA | title = A tyrosine-phosphorylated protein that binds to an important regulatory region on the cool family of p21-activated kinase-binding proteins | journal = The Journal of Biological Chemistry | volume = 274 | issue = 32 | pages = 22393–400 | date = August 1999 | pmid = 10428811 | doi = 10.1074/jbc.274.32.22393 }}</ref><ref name="RAA">{{cite journal | vauthors = Bagrodia S, Taylor SJ, Jordon KA, Van Aelst L, Cerione RA | title = A novel regulator of p21-activated kinases | journal = The Journal of Biological Chemistry | volume = 273 | issue = 37 | pages = 23633–6 | date = September 1998 | pmid = 9726964 | doi = 10.1074/jbc.273.37.23633 }}</ref> and by [[AP-1 transcription factor|AP1 transcription factor]].<ref>{{cite journal | vauthors = Holderness Parker N, Donninger H, Birrer MJ, Leaner VD | title = p21-activated kinase 3 (PAK3) is an AP-1 regulated gene contributing to actin organisation and migration of transformed fibroblasts | journal = PLoS One | volume = 8 | issue = 6 | pages = e66892 | date = 2013 | pmid = 23818969 | pmc = 3688571 | doi = 10.1371/journal.pone.0066892 }}</ref> Stimulation of PAK3 activity by upstream stimulators such as Dbl or Cdc42 is inhibited by p50 (Cool-1)<ref name="RAA" /> PAK3 activity is inhibited by FRAX597, a PAN inhibitor of PAKs.<ref>{{cite journal | vauthors = Licciulli S, Maksimoska J, Zhou C, Troutman S, Kota S, Liu Q, Duron S, Campbell D, Chernoff J, Field J, Marmorstein R, Kissil JL | title = FRAX597, a small molecule inhibitor of the p21-activated kinases, inhibits tumorigenesis of neurofibromatosis type 2 (NF2)-associated Schwannomas | journal = The Journal of Biological Chemistry | volume = 288 | issue = 40 | pages = 29105–14 | date = October 2013 | pmid = 23960073 | pmc = 3790009 | doi = 10.1074/jbc.m113.510933 }}</ref>
| image = PBB_Protein_PAK3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1e0a.
| PDB = {{PDB2|1e0a}}, {{PDB2|1ees}}, {{PDB2|1f3m}}, {{PDB2|1yhv}}, {{PDB2|1yhw}}, {{PDB2|2hy8}}
| Name = P21 (CDKN1A)-activated kinase 3
| HGNCid = 8592
| Symbol = PAK3
| AltSymbols =; CDKN1A; MRX30; MRX47; OPHN3; PAK3beta; bPAK; hPAK3
| OMIM = 300142
| ECnumber =
| Homologene = 55664
| MGIid = 1339656
| GeneAtlas_image1 = PBB_GE_PAK3_214607_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component =  
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5063
    | Hs_Ensembl = ENSG00000077264
    | Hs_RefseqProtein = NP_002569
    | Hs_RefseqmRNA = NM_002578
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = X
    | Hs_GenLoc_start = 110226244
    | Hs_GenLoc_end = 110350815
    | Hs_Uniprot = O75914
    | Mm_EntrezGene = 18481
    | Mm_Ensembl = ENSMUSG00000031284
    | Mm_RefseqmRNA = NM_008778
    | Mm_RefseqProtein = NP_032804
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = X
    | Mm_GenLoc_start = 138765079
    | Mm_GenLoc_end = 139038221
    | Mm_Uniprot = Q61036
  }}
}}
'''P21 (CDKN1A)-activated kinase 3''', also known as '''PAK3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PAK3 p21 (CDKN1A)-activated kinase 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5063| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
== Functions ==
{{PBB_Summary
PAK3 is overexpressed in neuroendocrine/carcinoids [[Neoplasm|tumors]].<ref>{{cite journal | vauthors = Liu RX, Wang WQ, Ye L, Bi YF, Fang H, Cui B, Zhou WW, Dai M, Zhang J, Li XY, Ning G | title = p21-activated kinase 3 is overexpressed in thymic neuroendocrine tumors (carcinoids) with ectopic ACTH syndrome and participates in cell migration | journal = Endocrine | volume = 38 | issue = 1 | pages = 38–47 | date = August 2010 | pmid = 20960100 | doi = 10.1007/s12020-010-9324-6 }}</ref> PAK3 has been shown to be important for synapse formation and plasticity, and contribute to mental retardation.<ref name="D" /> Further, a [[point mutation]] in PAK3 gene has been associated with nonsyndromic X-linked mental retardation.<ref name="CA" />
| section_title =  
| summary_text = PAK proteins are critical effectors that link Rho GTPases to cytoskeleton reorganization and nuclear signaling. PAK proteins, a family of serine/threonine p21-activating kinases, serve as targets for the small GTP binding proteins Cdc42 and RAC and have been implicated in a wide range of biological activities. The protein encoded by this gene forms an activated complex with GTP-bound RAS-like (P21), CDC2 and RAC1 proteins which then catalyzes a variety of targets. This protein may be necessary for dendritic development and for the rapid cytoskeletal reorganization in dendritic spines associated with synaptic plasticity. A point mutation in this gene has been linked to nonsyndromic X-linked mental retardation.<ref name="entrez">{{cite web | title = Entrez Gene: PAK3 p21 (CDKN1A)-activated kinase 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5063| accessdate = }}</ref>
}}


==References==
==Notes==
{{reflist|2}}
{{Academic-written review
==Further reading==
| wikidate = 2016
{{refbegin | 2}}
| journal = [[Gene (journal)|Gene]]
{{PBB_Further_reading
| title   = {{#property:P1476|from=Q38779105}}
| citations =  
| authors = {{#property:P2093|from=Q38779105}}
*{{cite journal | author=Bagrodia S, Cerione RA |title=Pak to the future. |journal=Trends Cell Biol. |volume=9 |issue= 9 |pages= 350-5 |year= 1999 |pmid= 10461188 |doi=  }}
| date    = {{#property:P577|from=Q38779105}}
*{{cite journal  | author=Illarioshkin SN, Tanaka H, Markova ED, ''et al.'' |title=X-linked nonprogressive congenital cerebellar hypoplasia: clinical description and mapping to chromosome Xq. |journal=Ann. Neurol. |volume=40 |issue= 1 |pages= 75-83 |year= 1996 |pmid= 8687195 |doi= 10.1002/ana.410400113 }}
| volume  = {{#property:P478|from=Q38779105}}
*{{cite journal  | author=Donnelly AJ, Partington MW, Ryan AK, Mulley JC |title=Regional localisation of two non-specific X-linked mental retardation genes (MRX30 and MRX31). |journal=Am. J. Med. Genet. |volume=64 |issue= 1 |pages= 113-20 |year= 1996 |pmid= 8826460 |doi= 10.1002/(SICI)1096-8628(19960712)64:1<113::AID-AJMG19>3.0.CO;2-Q }}
| issue   = {{#property:P433|from=Q38779105}}
*{{cite journal  | author=Siow YL, Kalmar GB, Sanghera JS, ''et al.'' |title=Identification of two essential phosphorylated threonine residues in the catalytic domain of Mekk1. Indirect activation by Pak3 and protein kinase C. |journal=J. Biol. Chem. |volume=272 |issue= 12 |pages= 7586-94 |year= 1997 |pmid= 9065412 |doi=  }}
| pages   = {{#property:P304|from=Q38779105}}
*{{cite journal  | author=Diaz B, Barnard D, Filson A, ''et al.'' |title=Phosphorylation of Raf-1 serine 338-serine 339 is an essential regulatory event for Ras-dependent activation and biological signaling. |journal=Mol. Cell. Biol. |volume=17 |issue= 8 |pages= 4509-16 |year= 1997 |pmid= 9234708 |doi=  }}
| doi     = {{#property:P356|from=Q38779105}}
*{{cite journal  | author=des Portes V, Soufir N, Carrié A, ''et al.'' |title=Gene for nonspecific X-linked mental retardation (MRX 47) is located in Xq22.3-q24. |journal=Am. J. Med. Genet. |volume=72 |issue= 3 |pages= 324-8 |year= 1997 |pmid= 9332663 |doi=  }}
| pmid   = {{#property:P698|from=Q38779105}}
*{{cite journal  | author=Manser E, Loo TH, Koh CG, ''et al.'' |title=PAK kinases are directly coupled to the PIX family of nucleotide exchange factors. |journal=Mol. Cell |volume=1 |issue= 2 |pages= 183-92 |year= 1998 |pmid= 9659915 |doi= }}
| pmc    = {{#property:P932|from=Q38779105}}
*{{cite journal  | author=Van Eyk JE, Arrell DK, Foster DB, ''et al.'' |title=Different molecular mechanisms for Rho family GTPase-dependent, Ca2+-independent contraction of smooth muscle. |journal=J. Biol. Chem. |volume=273 |issue= 36 |pages= 23433-9 |year= 1998 |pmid= 9722579 |doi=  }}
*{{cite journal  | author=Bagrodia S, Taylor SJ, Jordon KA, ''et al.'' |title=A novel regulator of p21-activated kinases. |journal=J. Biol. Chem. |volume=273 |issue= 37 |pages= 23633-6 |year= 1998 |pmid= 9726964 |doi=  }}
*{{cite journal  | author=Allen KM, Gleeson JG, Bagrodia S, ''et al.'' |title=PAK3 mutation in nonsyndromic X-linked mental retardation. |journal=Nat. Genet. |volume=20 |issue= 1 |pages= 25-30 |year= 1998 |pmid= 9731525 |doi= 10.1038/1675 }}
*{{cite journal  | author=King AJ, Sun H, Diaz B, ''et al.'' |title=The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338. |journal=Nature |volume=396 |issue= 6707 |pages= 180-3 |year= 1998 |pmid= 9823899 |doi= 10.1038/24184 }}
*{{cite journal  | author=Mason CS, Springer CJ, Cooper RG, ''et al.'' |title=Serine and tyrosine phosphorylations cooperate in Raf-1, but not B-Raf activation. |journal=EMBO J. |volume=18 |issue= 8 |pages= 2137-48 |year= 1999 |pmid= 10205168 |doi= 10.1093/emboj/18.8.2137 }}
*{{cite journal  | author=Premont RT, Claing A, Vitale N, ''et al.'' |title=The GIT family of ADP-ribosylation factor GTPase-activating proteins. Functional diversity of GIT2 through alternative splicing. |journal=J. Biol. Chem. |volume=275 |issue= 29 |pages= 22373-80 |year= 2000 |pmid= 10896954 |doi=  }}
*{{cite journal  | author=Bienvenu T, des Portes V, McDonell N, ''et al.'' |title=Missense mutation in PAK3, R67C, causes X-linked nonspecific mental retardation. |journal=Am. J. Med. Genet. |volume=93 |issue= 4 |pages= 294-8 |year= 2001 |pmid= 10946356 |doi= }}
*{{cite journal  | author=Hashimoto S, Tsubouchi A, Mazaki Y, Sabe H |title=Interaction of paxillin with p21-activated Kinase (PAK). Association of paxillin alpha with the kinase-inactive and the Cdc42-activated forms of PAK3. |journal=J. Biol. Chem. |volume=276 |issue= 8 |pages= 6037-45 |year= 2001 |pmid= 11096073 |doi= 10.1074/jbc.M005854200 }}
*{{cite journal  | author=Chiloeches A, Mason CS, Marais R |title=S338 phosphorylation of Raf-1 is independent of phosphatidylinositol 3-kinase and Pak3. |journal=Mol. Cell. Biol. |volume=21 |issue= 7 |pages= 2423-34 |year= 2001 |pmid= 11259591 |doi= 10.1128/MCB.21.7.2423-2434.2001 }}
*{{cite journal  | author=Chong C, Tan L, Lim L, Manser E |title=The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity. |journal=J. Biol. Chem. |volume=276 |issue= 20 |pages= 17347-53 |year= 2001 |pmid= 11278486 |doi= 10.1074/jbc.M009316200 }}
*{{cite journal  | author=Stoletov KV, Ratcliffe KE, Spring SC, Terman BI |title=NCK and PAK participate in the signaling pathway by which vascular endothelial growth factor stimulates the assembly of focal adhesions. |journal=J. Biol. Chem. |volume=276 |issue= 25 |pages= 22748-55 |year= 2001 |pmid= 11278553 |doi= 10.1074/jbc.M009720200 }}
*{{cite journal  | author=Yoshimura M, Homma K, Saito J, ''et al.'' |title=Dual regulation of mammalian myosin VI motor function. |journal=J. Biol. Chem. |volume=276 |issue= 43 |pages= 39600-7 |year= 2001 |pmid= 11517222 |doi= 10.1074/jbc.M105080200 }}
}}
}}
{{refend}}


{{protein-stub}}
== References ==
{{WikiDoc Sources}}
{{Reflist}}

Latest revision as of 00:13, 6 September 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

PAK3 (p21-activated kinase 2, beta-PAK) is one of three members of Group I PAK family of evolutionary conserved serine/threonine kinases.[1][2][3] PAK3 is preferentially expressed in neuronal cells [4][5] and involved in synapse formation and plasticity and mental retardation.[6][7]

Discovery

PAK3 was initially cloned from a murine fibroblast cDNA library and from a murine embryo cDNA library.[4][5] Like other group I PAKs, PAK3 is stimulated by activated Cdc42 and Rac1.

Gene and spliced variants

The human PAK3 gene, the longest group I family member, is 283-kb long. The PAK3 gene is composed of 22 exons of which 6 exons are for 5’-UTR and generates 13 alternative spliced transcripts. Among PAK3 transcripts, 11 transcripts are for coding proteins ranging from 181- to 580-amino acids long, while remaining two transcripts are non-coding RNAs.[8] The murine PAK3 gene contains 10 transcripts, coding six proteins from 544 amino acids and 559 amino acids long, and four smaller polypeptides from 23 to 366 amino acids.

Protein domains

Similar to PAK1, PAK2 contains a p21-binding domain (PBD) and an auto-inhibitory domain (AID) and exists in an inactive conformation.[9]

Activators and inhibitors

PAK3 activity is stimulated by Dbl, Cdc42 and Cool-2,[10][11] and by AP1 transcription factor.[12] Stimulation of PAK3 activity by upstream stimulators such as Dbl or Cdc42 is inhibited by p50 (Cool-1)[11] PAK3 activity is inhibited by FRAX597, a PAN inhibitor of PAKs.[13]

Functions

PAK3 is overexpressed in neuroendocrine/carcinoids tumors.[14] PAK3 has been shown to be important for synapse formation and plasticity, and contribute to mental retardation.[6] Further, a point mutation in PAK3 gene has been associated with nonsyndromic X-linked mental retardation.[7]

Notes


References

  1. ↑ Knaus UG, Morris S, Dong HJ, Chernoff J, Bokoch GM (July 1995). "Regulation of human leukocyte p21-activated kinases through G protein--coupled receptors". Science. 269 (5221): 221–3. doi:10.1126/science.7618083. PMID 7618083.
  2. ↑ Manser E, Chong C, Zhao ZS, Leung T, Michael G, Hall C, Lim L (October 1995). "Molecular cloning of a new member of the p21-Cdc42/Rac-activated kinase (PAK) family". The Journal of Biological Chemistry. 270 (42): 25070–8. doi:10.1074/jbc.270.42.25070. PMID 7559638.
  3. ↑ Kumar A, Molli PR, Pakala SB, Bui Nguyen TM, Rayala SK, Kumar R (July 2009). "PAK thread from amoeba to mammals". Journal of Cellular Biochemistry. 107 (4): 579–85. doi:10.1002/jcb.22159. PMC 2718766. PMID 19350548.
  4. ↑ 4.0 4.1 Bagrodia S, Taylor SJ, Creasy CL, Chernoff J, Cerione RA (September 1995). "Identification of a mouse p21Cdc42/Rac activated kinase". The Journal of Biological Chemistry. 270 (39): 22731–7. doi:10.1074/jbc.270.39.22731. PMID 7559398.
  5. ↑ 5.0 5.1 Burbelo PD, Kozak CA, Finegold AA, Hall A, Pirone DM (May 1999). "Cloning, central nervous system expression and chromosomal mapping of the mouse PAK-1 and PAK-3 genes". Gene. 232 (2): 209–15. doi:10.1016/s0378-1119(99)00110-9. PMID 10352232.
  6. ↑ 6.0 6.1 Boda B, Alberi S, Nikonenko I, Node-Langlois R, Jourdain P, Moosmayer M, Parisi-Jourdain L, Muller D (December 2004). "The mental retardation protein PAK3 contributes to synapse formation and plasticity in hippocampus". The Journal of Neuroscience. 24 (48): 10816–25. doi:10.1523/jneurosci.2931-04.2004. PMID 15574732.
  7. ↑ 7.0 7.1 Allen KM, Gleeson JG, Bagrodia S, Partington MW, MacMillan JC, Cerione RA, Mulley JC, Walsh CA (September 1998). "PAK3 mutation in nonsyndromic X-linked mental retardation". Nature Genetics. 20 (1): 25–30. doi:10.1038/1675. PMID 9731525.
  8. ↑ Kreis P, Rousseau V, Thévenot E, Combeau G, Barnier JV (August 2008). "The four mammalian splice variants encoded by the p21-activated kinase 3 gene have different biological properties". Journal of Neurochemistry. 106 (3): 1184–97. doi:10.1111/j.1471-4159.2008.05474.x. PMID 18507705.
  9. ↑ Kumar R, Li DQ (2016). PAKs in Human Cancer Progression: From Inception to Cancer Therapeutic to Future Oncobiology. Advances in Cancer Research. 130. pp. 137–209. doi:10.1016/bs.acr.2016.01.002. ISBN 9780128047897. PMID 27037753.
  10. ↑ Bagrodia S, Bailey D, Lenard Z, Hart M, Guan JL, Premont RT, Taylor SJ, Cerione RA (August 1999). "A tyrosine-phosphorylated protein that binds to an important regulatory region on the cool family of p21-activated kinase-binding proteins". The Journal of Biological Chemistry. 274 (32): 22393–400. doi:10.1074/jbc.274.32.22393. PMID 10428811.
  11. ↑ 11.0 11.1 Bagrodia S, Taylor SJ, Jordon KA, Van Aelst L, Cerione RA (September 1998). "A novel regulator of p21-activated kinases". The Journal of Biological Chemistry. 273 (37): 23633–6. doi:10.1074/jbc.273.37.23633. PMID 9726964.
  12. ↑ Holderness Parker N, Donninger H, Birrer MJ, Leaner VD (2013). "p21-activated kinase 3 (PAK3) is an AP-1 regulated gene contributing to actin organisation and migration of transformed fibroblasts". PLoS One. 8 (6): e66892. doi:10.1371/journal.pone.0066892. PMC 3688571. PMID 23818969.
  13. ↑ Licciulli S, Maksimoska J, Zhou C, Troutman S, Kota S, Liu Q, Duron S, Campbell D, Chernoff J, Field J, Marmorstein R, Kissil JL (October 2013). "FRAX597, a small molecule inhibitor of the p21-activated kinases, inhibits tumorigenesis of neurofibromatosis type 2 (NF2)-associated Schwannomas". The Journal of Biological Chemistry. 288 (40): 29105–14. doi:10.1074/jbc.m113.510933. PMC 3790009. PMID 23960073.
  14. ↑ Liu RX, Wang WQ, Ye L, Bi YF, Fang H, Cui B, Zhou WW, Dai M, Zhang J, Li XY, Ning G (August 2010). "p21-activated kinase 3 is overexpressed in thymic neuroendocrine tumors (carcinoids) with ectopic ACTH syndrome and participates in cell migration". Endocrine. 38 (1): 38–47. doi:10.1007/s12020-010-9324-6. PMID 20960100.
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