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P a r t i c i p a n t s :<br />
Silvia Bonaccorsi, Maria Grazia Giansanti, Patrizia<br />
Somma, Fiammetta Vernì, researchers; Elisabetta<br />
Bucciarelli, Gianluca Cestra, post-doc fellows; Claudia<br />
Pellacani, PhD student; Giorgio Belloni, technician.<br />
C o l l a b o r a t i o n s :<br />
Stanford University, USA (Prof. Margareth Fuller); Cornell<br />
University, USA (Prof. Michel L. Goldberg).<br />
Report of activity<br />
During animal cell cytokinesis, constriction of the<br />
acto-myosin ring leads to the formation of a furrow<br />
in the plasma membrane, which invaginates until the<br />
two daughter cells remain connected by a thin cytoplasmic<br />
bridge, called the midbody. This bridge is<br />
ultimately cleaved during the final step of cytokinesis,<br />
named abscisssion, which results in the complete<br />
separation of daughter cells. Both cleavage furrow<br />
ingression and abscission require substantial membrane<br />
remodelling. Membrane addition to the invaginating<br />
furrow involves vesicle delivery through both<br />
the secretory and the endocytic pathways. In the<br />
secretory pathway, vesicles are transported from the<br />
endoplasmic reticulum (ER) to the Golgi and then to<br />
the plasma membrane. In the endocytic pathway,<br />
plasma membrane-derived vesicles proceed to the<br />
recycling endosome (RE), which directs them back to<br />
the plasma membrane.<br />
Our goal is elucidation of the molecular mechanisms<br />
underlying membrane addition at the advancing<br />
cleavage furrow of Drosophila spermatocytes. We<br />
have recently identified mutations in six genes<br />
required for furrow ingression during meiotic<br />
cytokinesis of Drosophila males. All these genes<br />
encode products involved in membrane trafficking:<br />
Zw10, Rab1, the Exocist complex components<br />
Exo84 and Sec8, and the ortholog of PACS-1. We<br />
plan to define the roles of these proteins in furrow<br />
Principal investigator: Maurizio Gatti<br />
Professor of Genetics<br />
Dipartimento di Genetica e Biologia Molecolare<br />
Tel: (+39) 06 49912842; Fax: (+39) 06 4456866<br />
maurizio.gatti@uniroma1.it<br />
51<br />
Molecular genetics of eukaryotes - AREA 3<br />
The role of membrane trafficking in Drosophila cytokinesis<br />
ingression, and investigate their functional relationships<br />
with other proteins involved in membrane traffic<br />
during cytokinesis.<br />
In the past two years we have carried out three main<br />
research projects.<br />
The role for of bond in furrow ingression<br />
during cytokinesis in Drosophila<br />
spermatocytes<br />
Recent work has shown that plasma membrane lipids<br />
influence membrane biophysical properties such as<br />
membrane curvature and elasticity and play an active<br />
role in cell function. We have found that mutations in<br />
the gene bond, which encodes a Drosophila member of<br />
the family of Elovl proteins that mediate elongation<br />
of very-long-chain fatty acids, block or dramatically<br />
slow cleavage-furrow ingression during early<br />
telophase in dividing spermatocytes. Bond shares<br />
sequence motifs with human and yeast Elovl family<br />
members, including five to seven predicted transmembrane<br />
domains, and can substitute for elovl<br />
genes in S. cerevisiae. In bond mutant cells at late<br />
stages of meiotic division, the contractile ring frequently<br />
detaches from the cortex and constricts or<br />
collapses to one side of the cell, and the cleavage furrow<br />
regresses. These findings implicate very-longchain<br />
fatty acids or their derivative complex lipids in<br />
allowing supple membrane deformation and the stable<br />
connection of cortical contractile components to<br />
the plasma membrane during cell division.<br />
brunelleschi (bru) is required to regulate<br />
Rab11 behavior during meiotic cytokinesis in<br />
Drosophila males<br />
We have found that successful furrow ingression during<br />
meiotic cytokinesis in Drosophila males requires<br />
function of the gene brunelleschi (bru), which encodes<br />
the ortholog of the yeast transport protein particle<br />
(TRAPP) II complex subunit, Trs120p. Dividing male<br />
meiotic cells from bru mutants assemble a normal contractile<br />
ring that initiates constriction but fails to con-