Is POPDC1 a potential target in multiple cancers?

Running head: MEDICAL
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1MEDICAL
Research Title: Is POPDC1 a potential target in multiple cancers?
Introduction:
POPDC protein are broadly referred to as Popeye domain containing proteins which
are a novel class of cAMP binding molecules. A number of research studies have shown that
these proteins can affect the cell behaviour of the cancerous cells and alter the related clinical
outcome. These proteins are encoded by the family of POPDC genes which includes the
POPDC1, POPDC2 and POPDC3 genes respectively (Schindler and Brand 2013). POPDC
proteins structurally comprise of three-pass transmembrane proteins which constitute of a
short amino-terminus that are characterized with two N-glycosylation sites (Schindler and
Brand 2013). The molecular weight of POPDC1 protein is equivalent to 42kDa. It should be
noted in this context that POPDC proteins form homo-dimers which are subsequently
stabilized by disulphide bonds and helps in the maintenance of epithelial and junction
integrity. A number of research studies suggest that conserved lysines at the corboxy-terminal
end of the popeye domain in POPDC1 protein regulate the function of homo-dimerization
(Brand et al. 2014). The C terminus of the POPDC protein is located within the cytoplasm
and comprises of the popeye domain which contains a high conserved region of 150 amino
acids (Brand et al. 2014).
It should be noted in this context that the popeye domain comprises of a functional
cyclic nucleotide binding domain which facilitates the specific binding to the adenosine 3’,5’-
cyclic monophosphate (CAMP). As per Schindler and Brand (2013), it has been stated that
POPDC proteins do not bind to cGMP as the affinity factor differs by the factor 40. It should
be noted here that POPDC proteins are the five classes of eukaryotic cAMP effector proteins
which are involved in the process of protein exchange activated by cAMP.