QUIROGA RODRIGO
Congresos y reuniones científicas
Título:
Characterization of the Complete set of SNAREs in the golgi-lacking eukaryote Giardia lamblia.
Autor/es:
ELÍAS, ELIANA VANINA; QUIROGA, RODRIGO; GOTTIG, NATALIA; LUJÁN, HUGO DANIEL
Lugar:
Carlos Paz, Córdoba, Argentina.
Reunión:
Congreso; XLIV Reunión Anual de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular (SAIB).; 2008
Institución organizadora:
SAIB
Resumen:
Giardia is an eukaryotic protozoan with unusual characteristics,
such as the absence of a morphologically evident Golgi apparatus.
Although both constitutive and regulated pathways for protein
secretion exist in Giardia, little is known about the molecules and
mechanisms involved in vesicular docking and fusion. In higher
eukaryotes, soluble N-ethylmaleimide-sensitive factor-attachment
protein receptors (SNAREs) of the vesicle-associated membrane
protein (VAMP) and Syntaxin families play essential roles in these
processes. An exhaustive search of the complete Giardia genome
identified genes for 17 SNARE proteins, some of which possess
atypical amino acids at the zero layer of the SNARE domain. The
expression and localization of all SNAREs demonstrate that specific
SNAREs localize to distinct subcellular organelles. Our results
suggest that these compartments represent the extent of the
endomembrane system in eukaryotes. Comparison of Giardia
SNAREs homologous to Golgi SNAREs from other organisms does
not allow the detection of a typical Golgi apparatus in trophozoites.
Moreover, depletion of individual genes demonstrated that several
SNAREs are essential for viability. Thus, Giardia requires a smaller
number of SNAREs, compared to other eukaryotes, to accomplish
all the vesicle trafficking events that are critical for growth and
differentiation of this important human pathogen.
such as the absence of a morphologically evident Golgi apparatus.
Although both constitutive and regulated pathways for protein
secretion exist in Giardia, little is known about the molecules and
mechanisms involved in vesicular docking and fusion. In higher
eukaryotes, soluble N-ethylmaleimide-sensitive factor-attachment
protein receptors (SNAREs) of the vesicle-associated membrane
protein (VAMP) and Syntaxin families play essential roles in these
processes. An exhaustive search of the complete Giardia genome
identified genes for 17 SNARE proteins, some of which possess
atypical amino acids at the zero layer of the SNARE domain. The
expression and localization of all SNAREs demonstrate that specific
SNAREs localize to distinct subcellular organelles. Our results
suggest that these compartments represent the extent of the
endomembrane system in eukaryotes. Comparison of Giardia
SNAREs homologous to Golgi SNAREs from other organisms does
not allow the detection of a typical Golgi apparatus in trophozoites.
Moreover, depletion of individual genes demonstrated that several
SNAREs are essential for viability. Thus, Giardia requires a smaller
number of SNAREs, compared to other eukaryotes, to accomplish
all the vesicle trafficking events that are critical for growth and
differentiation of this important human pathogen.
