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Title 

Cysteine repeat domains and adjacent sequences determine distinct bone morphogenetic protein modulatory activities of the drosophila sog protein

Authors 

Kweon YuK H KangP HeineU PyatiS SrinivasanB BiehsD KimelmanE Bier

Publisher 

Genetics Society of America

Issue Date 

2004

Citation 

Genetics, vol. 166, no. 3, pp. 1323-1336

Keywords 

bone morphogenetic proteincysteinedrosophila proteinprotein Sogamino acid sequencedrosophilaprotein domainprotein protein interactionbone morphogenetic proteinsprotein structure, tertiary

Abstract 

The Drosophila short gastrulation gene (sog) encodes a large extracellular protein (Sog) that inhibits signaling by BMP-related ligands. Sog and its vertebrate counterpart Chordin contain four copies of a cysteine repeat (CR) motif defined by 10 cysteine residues spaced in a fixed pattern and a tryptophan residue situated between the first two cysteines. Here we present a structure-function analysis of the CR repeats in Sog, using a series of deletion and point mutation constructs, as well as constructs in which CR domains have been swapped. This analysis indicates that the CR domains are individually dispensable for Sog function but that they are not interchangeable. These studies reveal three different types of Sog activity: intact Sog, which inhibits signaling mediated by the ligand Glass bottom boat (Gbb), a more broadly active class of BMP antagonist referred to as Supersog, and a newly identified activity, which may promote rather than inhibit BMP signaling. Analysis of the activities of CR swap constructs indicates that the CR domains are required for full activity of the various forms of Sog but that the type of Sog activity is determined primarily by surrounding protein sequences. Cumulatively, our analysis suggests that CR domains interact physically with adjacent protein sequences to create forms of Sog with distinct BMP modulatory activities.

ISSN 

0016-6731

Link 

http://dx.doi.org/10.1534/genetics.166.3.1323

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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