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PIKE GTPase are phosphoinositide-3-kinase enhancers, suppressing programmed cell death.

Chan CB, Ye K - J. Cell. Mol. Med. (2007 Jan-Feb)

Bottom Line: PIKE-A does not interplay with PI3K.Instead, it interacts with the downstream effector Akt and promotes its activity.Because both PI3K and Akt are important effectors in the growth factor-mediated signaling which triggers cellular growth and acts against apoptosis, PIKEs therefore serve as the molecular switch that their activation are crucial for growth factors to exert their physiological functions.

View Article: PubMed Central - PubMed

Affiliation: Department of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, GA, USA.

ABSTRACT
Phosphoinositide-3-kinase enhancers (PIKE) are GTP-binding proteins that posses anti-apoptotic functions. The PIKE family includes three members, PIKE-L, PIKE-S and PIKE-A, which are originated from a single gene (CENTG1) through alternative splicing or differential transcription initiation. Both PIKE-S and PIKE-L bind to phosphoinositide-3-kinase (PI3K) and enhance its activity. PIKE-A does not interplay with PI3K. Instead, it interacts with the downstream effector Akt and promotes its activity. These actions are mediated by their GTPase activity. Because both PI3K and Akt are important effectors in the growth factor-mediated signaling which triggers cellular growth and acts against apoptosis, PIKEs therefore serve as the molecular switch that their activation are crucial for growth factors to exert their physiological functions. In this review, the current understanding of different PIKE isoforms in growth factors-induced anti-apoptotic function will be discussed. Moreover, the role of PIKE in the survival and invasion activity of cancer cells will also be introduced.

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Structure of PIKE proteins. Schematic representations of PIKE proteins (A) and partial alignment of the PH domains of rat PIKEs amino acids (B) were shown. The structure which is different from that of other isoforms in PIKE-A is shown in red. Identical amino acids were marked with an asterisk and the corresponding position of the amino acid in each protein was numbered.
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fig01: Structure of PIKE proteins. Schematic representations of PIKE proteins (A) and partial alignment of the PH domains of rat PIKEs amino acids (B) were shown. The structure which is different from that of other isoforms in PIKE-A is shown in red. Identical amino acids were marked with an asterisk and the corresponding position of the amino acid in each protein was numbered.

Mentions: PIKE proteins are GTP-binding proteins which contain three members, PIKE-S, PIKE-L and PIKE-A (Fig. 1). They are originated from a single gene, CENTG1, by alternative splicing (PIKE-S and PIKE-L) or differential transcription start site usage (PIKE-A) [21, 22]. PIKE-S contains three praline-rich domains (PRD) at the N-terminus, followed by a GTP-binding motif (the GTPase region) and a PH domain. PIKE-L is the longer isoform of PIKE-S which possesses an extra C-terminal extension that includes a domain showing sequence homology to ARF/GAP protein (Arf-GAP) and two ankyrin repeats (ANK). PIKE-A shares identical structure with PIKE-L at the C-terminal but differ at the N-terminal that PIKE-A has no PRD.


PIKE GTPase are phosphoinositide-3-kinase enhancers, suppressing programmed cell death.

Chan CB, Ye K - J. Cell. Mol. Med. (2007 Jan-Feb)

Structure of PIKE proteins. Schematic representations of PIKE proteins (A) and partial alignment of the PH domains of rat PIKEs amino acids (B) were shown. The structure which is different from that of other isoforms in PIKE-A is shown in red. Identical amino acids were marked with an asterisk and the corresponding position of the amino acid in each protein was numbered.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4401219&req=5

fig01: Structure of PIKE proteins. Schematic representations of PIKE proteins (A) and partial alignment of the PH domains of rat PIKEs amino acids (B) were shown. The structure which is different from that of other isoforms in PIKE-A is shown in red. Identical amino acids were marked with an asterisk and the corresponding position of the amino acid in each protein was numbered.
Mentions: PIKE proteins are GTP-binding proteins which contain three members, PIKE-S, PIKE-L and PIKE-A (Fig. 1). They are originated from a single gene, CENTG1, by alternative splicing (PIKE-S and PIKE-L) or differential transcription start site usage (PIKE-A) [21, 22]. PIKE-S contains three praline-rich domains (PRD) at the N-terminus, followed by a GTP-binding motif (the GTPase region) and a PH domain. PIKE-L is the longer isoform of PIKE-S which possesses an extra C-terminal extension that includes a domain showing sequence homology to ARF/GAP protein (Arf-GAP) and two ankyrin repeats (ANK). PIKE-A shares identical structure with PIKE-L at the C-terminal but differ at the N-terminal that PIKE-A has no PRD.

Bottom Line: PIKE-A does not interplay with PI3K.Instead, it interacts with the downstream effector Akt and promotes its activity.Because both PI3K and Akt are important effectors in the growth factor-mediated signaling which triggers cellular growth and acts against apoptosis, PIKEs therefore serve as the molecular switch that their activation are crucial for growth factors to exert their physiological functions.

View Article: PubMed Central - PubMed

Affiliation: Department of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, GA, USA.

ABSTRACT
Phosphoinositide-3-kinase enhancers (PIKE) are GTP-binding proteins that posses anti-apoptotic functions. The PIKE family includes three members, PIKE-L, PIKE-S and PIKE-A, which are originated from a single gene (CENTG1) through alternative splicing or differential transcription initiation. Both PIKE-S and PIKE-L bind to phosphoinositide-3-kinase (PI3K) and enhance its activity. PIKE-A does not interplay with PI3K. Instead, it interacts with the downstream effector Akt and promotes its activity. These actions are mediated by their GTPase activity. Because both PI3K and Akt are important effectors in the growth factor-mediated signaling which triggers cellular growth and acts against apoptosis, PIKEs therefore serve as the molecular switch that their activation are crucial for growth factors to exert their physiological functions. In this review, the current understanding of different PIKE isoforms in growth factors-induced anti-apoptotic function will be discussed. Moreover, the role of PIKE in the survival and invasion activity of cancer cells will also be introduced.

Show MeSH
Related in: MedlinePlus