Ask about this productRelated genes to: PAK6 antibody
- Gene:
- PAK2 NIH gene
- Name:
- p21 (RAC1) activated kinase 2
- Previous symbol:
- -
- Synonyms:
- PAK65, PAKgamma
- Chromosome:
- 3q29
- Locus Type:
- gene with protein product
- Date approved:
- 1998-03-25
- Date modifiied:
- 2016-10-24
- Gene:
- PAK6 NIH gene
- Name:
- p21 (RAC1) activated kinase 6
- Previous symbol:
- -
- Synonyms:
- PAK5
- Chromosome:
- 15q15.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-07-12
- Date modifiied:
- 2016-10-05
Related products to: PAK6 antibody
Related articles to: PAK6 antibody
- There is a dearth of knowledge regarding transmission of () and () species through water and water-related sources in Pakistan. To this end, we conducted a study to evaluate the prevalence of these parasites in different water bodies, soil, and mixed raw vegetables in Pakistan. Researchers collected 200 samples from each reservoir including municipal water, sewage water, canal water, raw vegetables, soil of public parks, and soil of grazing areas. Researchers amplified the 18S ribosomal RNA gene of parasites using newly designed genus-specific primers through polymerase chain reaction testing. The sequencing analysis revealed that the obtained sequences belonged to and . Phylogenetic clustering and sequence analysis of showed that the Pak1 (OM540369) and Pak2 (OM540370) as well as Pak3 (OM510450) and Pak6 (OM510445) were closely similar to each other. In the case of , all the sequences appeared in the same clade. The epidemiological data showed lower prevalence of (11.5%) in all reservoirs, compared with (20.5%). Among different reservoirs, prevalence of and was observed in sewage water ( = 13%, = 26.5%), municipal water ( = 10%, = 35%), canal water ( = 9.5%, = 18.5%), raw vegetables ( = 5.5%, = 8%), soil of public parks ( = 13%, = 14%), and soil of grazing areas ( = 18.5%, = 21.5%). Among targeted risk factors, poor hygienic conditions significantly affected the prevalence of parasites in sewage water ( = 20%, = 41.2%), municipal water ( = 14.7%, = 48.8.5%), raw vegetables ( = 11.3%, = 15.1%), and soil of public parks ( = 19.5%, = 21.9%). Similarly, contamination with sewage waste significantly affected ( < .05) the prevalence of these parasites in municipal water ( = 13.6%, = 41.1%), canal water ( = 13.3%, = 25%), raw vegetables ( = 12.1%, = 15.1%), and soil of public parks ( = 23.3%, = 15%). Results of this study illustrated a high risk of parasitic zoonosis through water bodies, soil, and vegetables. - Source: PubMed
Publication date: 2022/07/20
Abbas ZaheerKhan Muhammad KasibAbbas Rao ZahidSindhu Zia Ud DinSajid Muhammad SohailMunir AmirWahid AbdulZafar ArsalanMughal Muhammad Adnan SabirImran MuhammadMehmood RashidNadeem Muhammad - PAKs (p21-activated kinases) are reported to play crucial roles in a variety of cellular processes and participate in the progression of human cancers. However, the expression and prognostic values of PAKs remain poorly explored in breast cancers. In our study, we examined the mRNA and protein expression levels of PAKs and the prognostic value. We also analyzed the interaction network, genetic alteration, and functional enrichment of PAKs. The results showed that the mRNA levels of PAK1, PAK2, PAK4 and PAK6 were significantly up-regulated in breast cancer compared with normal tissues, while the reverse trend for PAK3 and PAK5 was found, furthermore, the proteins expression of PAK1, PAK2 and PAK4 in breast cancer tissues were higher than that in normal breast tissues. Survival analysis revealed breast cancer patients with low mRNA expression of PAK3 and PAK5 showed worse RFS, conversely, elevated PAK4 levels predicted worse RFS. In addition, the breast cancer patients with PAKs genetic alterations correlated with worse OS. These results indicated that PAKs might be promising potential biomarkers for breast cancer. - Source: PubMed
Publication date: 2020/01/24
Dang YifangGuo YingMa XiaoyuChao XiaoyuWang FeiCai LinghaoYan ZhongyiXie LongxiangGuo Xiangqian - p21-activated kinases (PAKs) are serine/threonine kinase effectors of the small GTPases Rac and Cdc42 and major participants in cell adhesion, motility, and survival. Type II PAKs (PAK4, -5, and -6) are recruited to cell-cell boundaries, where they regulate adhesion dynamics and colony escape. In contrast, the type I PAK, PAK1, does not localize to cell-cell contacts. We have now found that the other type I PAKs (PAK2 and PAK3) also fail to target to cell-cell junctions. PAKs contain extensive similarities in sequence and domain organization; therefore, focusing on PAK1 and PAK6, we used chimeras and truncation mutants to investigate their differences in localization. We observed that a weakly conserved sequence region (the variable region), located between the Cdc42-binding CRIB domain and the kinase domain, inhibits PAK1 targeting to cell-cell junctions. Accordingly, substitution of the PAK1 variable region with that from PAK6 or removal of this region of PAK1 resulted in its localization to cell-cell contacts. We further show that Cdc42 binding is required, but not sufficient, to direct PAKs to cell-cell contacts and that an N-terminal polybasic sequence is necessary for PAK1 recruitment to cell-cell contacts, but only if the variable region-mediated inhibition is released. We propose that all PAKs contain cell-cell boundary-targeting motifs but that the variable region prevents type I PAK accumulation at junctions. This highlights the importance of this poorly conserved, largely disordered region in PAK regulation and raises the possibility that variable region inhibition may be released by cellular signals. - Source: PubMed
Publication date: 2019/08/07
Sun XiaowenSu Valerie LCalderwood David A - Atypical RhoV GTPase (Chp/Wrch-2) is a member of the human Rho GTPase family, which belongs to the superfamily of Ras-related small GTPases. The biological functions of RhoV, regulation of its activity, and mechanisms of its action remain largely unexplored. Rho GTPases regulate a wide range of cellular processes by interacting with protein targets called effectors. Several putative RhoV effectors have been identified, including protein kinases of the Pak (p21-activated kinase) family: Pak1, Pak2, Pak4, and Pak6. RhoV GTPase activates Pak1 protein kinase and simultaneously induces its ubiquitin-dependent degradation. Pak1 regulates E-cadherin localization at adherens junctions downstream of RhoV during gastrulation in fish. The effector domain of RhoV mediates its binding to the CRIB (Cdc42/Rac1 interactive binding) motif in the N-terminal p21-binding domain (PBD) of Pak6 protein kinase. The role of the RhoV effector domain in mediating interaction with Pak1 has not been studied. This study has identified mutations in the effector domain of RhoV GTPase (Y60K, T63A, L65A, and D66A) that impair its interaction with Pak1 in the GST-PAK-PBD pull-down assay and coimmunoprecipitation. Our results suggest that the effector domain of RhoV mediates its binding to Pak1, complementing the current view of the molecular basics of RhoV binding to effectors of the Pak family. These data lay the basis for further studies on the role of Pak1 in RhoV-activated signaling pathways and cellular processes. - Source: PubMed
Korobko I VShepelev M V - The p21-activated kinases (PAKs) are a family of six serine/threonine kinases that act as key effectors of RHO family GTPases in mammalian cells. PAKs are subdivided into two groups: type I PAKs (PAK1, PAK2, and PAK3) and type II PAKs (PAK4, PAK5, and PAK6). Although these groups are involved in common signaling pathways, recent work indicates that the two groups have distinct modes of regulation and have both unique and common substrates. Here, we review recent insights into the molecular level details that govern regulation of type II PAK signaling. We also consider mechanisms by which signal transduction is regulated at the level of substrate specificity. Finally, we discuss the implications of these studies for clinical targeting of these kinases. - Source: PubMed
Publication date: 2015/04/08
Ha Byung HakMorse Elizabeth MTurk Benjamin EBoggon Titus J