TY - JOUR
T1 - Protein prenylation
T2 - A new mode of host-pathogen interaction
AU - Amaya, Moushimi
AU - Baranova, Ancha
AU - Van Hoek, Monique L.
PY - 2011/12/9
Y1 - 2011/12/9
N2 - Post translational modifications are required for proteins to be fully functional. The three step process, prenylation, leads to farnesylation or geranylgeranylation, which increase the hydrophobicity of the prenylated protein for efficient anchoring into plasma membranes and/or organellar membranes. Prenylated proteins function in a number of signaling and regulatory pathways that are responsible for basic cell operations. Well characterized prenylated proteins include Ras, Rac and Rho. Recently, pathogenic prokaryotic proteins, such as SifA and AnkB, have been shown to be prenylated by eukaryotic host cell machinery, but their functions remain elusive. The identification of other bacterial proteins undergoing this type of host-directed post-translational modification shows promise in elucidating host-pathogen interactions to develop new therapeutics. This review incorporates new advances in the study of protein prenylation into a broader aspect of biology with a focus on host-pathogen interaction.
AB - Post translational modifications are required for proteins to be fully functional. The three step process, prenylation, leads to farnesylation or geranylgeranylation, which increase the hydrophobicity of the prenylated protein for efficient anchoring into plasma membranes and/or organellar membranes. Prenylated proteins function in a number of signaling and regulatory pathways that are responsible for basic cell operations. Well characterized prenylated proteins include Ras, Rac and Rho. Recently, pathogenic prokaryotic proteins, such as SifA and AnkB, have been shown to be prenylated by eukaryotic host cell machinery, but their functions remain elusive. The identification of other bacterial proteins undergoing this type of host-directed post-translational modification shows promise in elucidating host-pathogen interactions to develop new therapeutics. This review incorporates new advances in the study of protein prenylation into a broader aspect of biology with a focus on host-pathogen interaction.
KW - AnkB
KW - Pathogenic bacteria
KW - Plasma membrane anchoring
KW - Prenylation
KW - SifA
UR - http://www.scopus.com/inward/record.url?scp=83055180495&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2011.10.142
DO - 10.1016/j.bbrc.2011.10.142
M3 - Short survey
C2 - 22079293
AN - SCOPUS:83055180495
SN - 0006-291X
VL - 416
SP - 1
EP - 6
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1-2
ER -