QUIROGA RODRIGO
Congresos y reuniones científicas
Título:
A NOVEL MOTIF AT THE C-TERMINUS OF PALMITOYLTRANSFERASES IS ESSENTIAL FOR SWF1 FUNCTION IN VIVO
Autor/es:
GONZÁLEZ MONTORO, AYELÉN; QUIROGA, RODRIGO; VALDEZ TAUBAS, JAVIER
Lugar:
Carlos Paz, Córdoba, Argentina.
Reunión:
Congreso; XLIV Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; 2008
Institución organizadora:
SAIB
Resumen:
S-acylation (also known as palmitoylation) is the addition of a lipid
molecule to cysteine residues of a protein through a thioester bond.
This modification is mediated by proteins referred to as
Palmitoyltransferases (PATs), characterised by the presence of a
conserved DHHC-Cysteine-Rich Domain. Swf1 is a yeast member
of the DHHC family, and it is responsible for the S-acylation of
several SNARES and other membrane proteins. Here we describe a
novel 16 amino acid motif, present at the cytosolic C-terminus of
PATs, that is required for Swf1 function in vivo. Within this motif,
we have identified a single residue in Swf1, Tyr-323, as essential for
function, and this is correlated with lack of palmitoylation of Tlg1, a
SNARE that is a substrate of Swf1. Substitution of Tyr-323 with
Alanine is the first phenotype affecting mutation uncovered that
does not lie within the DHHC domain, for this or any other PAT. In
silico analyses indicate that the motif is conserved in 70% of all
PATs, and suggest that the motif may have once been present in all
PATs. We named this motif ?Palmitoyltransferase Conserved C-
Terminus? (PaCCT). Additionally, while searching for a funtion for
the PaCCT domain, we obtained preliminary evidence indicating
that the Cytosolic C-terminus of Swf1 interacts with palmitoyl-
CoA, the lipid donor in S-acylaction, albeit independently of the
PaCCT domain.
molecule to cysteine residues of a protein through a thioester bond.
This modification is mediated by proteins referred to as
Palmitoyltransferases (PATs), characterised by the presence of a
conserved DHHC-Cysteine-Rich Domain. Swf1 is a yeast member
of the DHHC family, and it is responsible for the S-acylation of
several SNARES and other membrane proteins. Here we describe a
novel 16 amino acid motif, present at the cytosolic C-terminus of
PATs, that is required for Swf1 function in vivo. Within this motif,
we have identified a single residue in Swf1, Tyr-323, as essential for
function, and this is correlated with lack of palmitoylation of Tlg1, a
SNARE that is a substrate of Swf1. Substitution of Tyr-323 with
Alanine is the first phenotype affecting mutation uncovered that
does not lie within the DHHC domain, for this or any other PAT. In
silico analyses indicate that the motif is conserved in 70% of all
PATs, and suggest that the motif may have once been present in all
PATs. We named this motif ?Palmitoyltransferase Conserved C-
Terminus? (PaCCT). Additionally, while searching for a funtion for
the PaCCT domain, we obtained preliminary evidence indicating
that the Cytosolic C-terminus of Swf1 interacts with palmitoyl-
CoA, the lipid donor in S-acylaction, albeit independently of the
PaCCT domain.
