Previous report has indicated that CRMP2 is a key player in determining the localisation and trafficking posttranslational modification of CRMP2 can affect trafficking of Nav1 7 both positively or negatively Studies suggest that CRMP2 can interact with Nav1 7 causing SUMOlaytion to occurs which allows it to be phosphorylated by Cdk5 and this has proven to be obligatory for promoting positive regulation in the transport of channel to the plasma membrane When CRMP2 is detached from SUMO it can recruit scaffold protein Numb and be phosphorylated by Fyn and allow Nedd4 2 to bind hence allow internalisation of NaV1 7 Although CRMP2 can regulate Nav1 7 expression both ways the phosphorylation by Cdk5 was shown to be dominant over the phosphorylation by Fyn REF It is also noted that CRMP2 has a higher selectivity to Nav1 7 than other VGSC REF The reason for CRMP2 having a higher affinity to Nav1 7 is not fully understood one hypothesis is that CRMP2 have a higher affinity to the Nav1 7 intracellular domain that are not conserved in other isoforms
To investigate the involvement in of different intracellular parts of Nav1 7 in prostate cancer cells the trafficking potential of B1 B3 and B5 was examined by immunolabelling with two different antibodies As Cdk5 phosphorylation is dominant over Fyn phosphorylation an increase in trafficking is expected when Nav1 7 intracellular domain DNA is added to the CD4 protein The hypothesis that fusing the B5 intracellular parts of Nav1 7 to CD4 protein will result in increased trafficking of the channel was supported by the data Evaluation of the data described that there is a significant increase in trafficking by a mean of 23 suggesting that with the present of B5 intracellular parts the trafficking of Nav1 7 to the plasma membrane is increased This could suggest that CRMP2 might have a higher affinity to the B5 intracellular parts of Nav1 7 however no previous research has mapped the interaction between CRMP2 and Nav1 7 further investigation using mass spectrometry should be used to define the detailed protein protein interaction between these two proteins Surprisingly the result of B1 and B3 group did not demonstrate an increase in transport of the CD4 protein but a decrease was observed When comparing the B1 result to the control CD4 it indicted that there was a mean decrease of 27 0 in protein membrane trafficking Similar interpretation was obtained with the B3 group the mean membrane total ratio was illustrated to be 22 7 lower than that was recorded from the CD4 control group Results highlight that the B1 and B3 parts of the intracellular domain do negatively influence the trafficking in prostate cancer cell one possibility to explain this is that the binding of CRMP2 can negatively regulates the channel trafficking to cell membrane when it is bound to different proteins
Although it has convey that Cdk5 and Fyn serve as checkpoints that target CRMP2 and result with trafficking in opposing direction it is also known that phosphorylation by Cdk5 is dominant over the Fyn phosphorylation it must be noted that however the full mechanism of this pathway is still unknown and there could be a unidentified protein that participate in this pathway Moreover different molecules for example the beta subunit of the Nav1 7 protein kinase A and mitogen activated protein kinase are reported to be involved in the transport of Nav1 7 REF this highlight that the regulatory of the Nav1 7 trafficking system is complex therefore the chance of another molecule or pathway that are required to interact with the intracellular domain for full function cannot be eliminated When comparing result to experiment performed on other cell types trafficking potential were different for B1 B3 and B5 This could be due to different cell type environment protein that it has different in regulation In this experiment the main source of error is the identification of cells the identification and selection of cells are done manually and therefore a bias might have occur for cells with a stronger signal what we did to minimise the error Furthermore experiment different degree cells are biological different to each other Experimental skill different batch of antibody used no dapi added transfection efficiency cells might digested the protein made a role in transfection reagent What causes which pathway maybe try to find other things that are involved with Nav1 7 trafficking that could cause different result other factor that might have been involved the beta subunit other protein maybe a comparison of result between different cell type why would it has an effect why is it different in different cell types Experimental error suggestion to improve different transfection efficiency conclusion more to discover B1 B3 B5 have an effect on trafficking Different in different cell types cell environment composition need to be take in consideration What to do next
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