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Vol. 8, Issue 11, 2291-2306, November 1997
*Biozentrum of the University of Basel, CH-4056 Basel, Switzerland;
end4-1 was isolated as a temperature-sensitive
endocytosis mutant. We cloned and sequenced END4 and
found that it is identical to SLA2/MOP2. This gene is
required for growth at high temperature, viability in the absence of
Abp1p, polarization of the cortical actin cytoskeleton, and
endocytosis. We used a mutational analysis of END4 to
correlate in vivo functions with regions of End4p and we found that two
regions of End4p participate in endocytosis but that the talin-like
domain of End4p is dispensable. The N-terminal domain of End4p is
required for growth at high temperature, endocytosis, and actin
organization. A central coiled-coil domain of End4p is necessary for
formation of a soluble sedimentable complex. Furthermore, this domain
has an endocytic function that is redundant with the function(s) of
ABP1 and SRV2. The endocytic function of
Abp1p depends on its SH3 domain. In addition we have isolated a
recessive negative allele of SRV2 that is defective for
endocytosis. Combined biochemical, functional, and genetic analysis
lead us to propose that End4p may mediate endocytosis through
interaction with other actin-associated proteins, perhaps Rvs167p, a
protein essential for endocytosis.
Department of Biochemistry, Molecular Biology and Cell
Biology, Northwestern University, Evanston, Illinois;
Institut für Biochemie und Molekulare
Zellbiologie, University of Vienna, A-1030 Wien, Austria; and
§Institute of Molecular Agrobiology, Singapore
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