A conserved membrane-binding domain targets proteins to organelle contact sites | Zendy

Alexandre Toulmay | Zendy; William A. Prinz | Zendy

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A conserved membrane-binding domain targets proteins to organelle contact sites

Author(s) -

Alexandre Toulmay,

William A. Prinz

Publication year - 2012

Publication title -

journal of cell science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.384

H-Index - 278

eISSN - 1477-9137

pISSN - 0021-9533

DOI - 10.1242/jcs.085118

Subject(s) - biology , organelle , c2 domain , saccharomyces cerevisiae , membrane protein , microbiology and biotechnology , mitochondrial membrane transport protein , biochemistry , membrane contact site , yeast , conserved sequence , protein domain , binding domain , binding site , membrane , integral membrane protein , peptide sequence , gene

Membrane contact sites (MCSs), where the membranes of two organelles are closely apposed, are regions where small molecules such as lipids or calcium are exchanged between organelles. We have identified a conserved membrane-binding domain found exclusively in proteins at MCSs in Saccharomyces cerevisiae. The synaptotagmin-like-mitochondrial-lipid binding protein (SMP) domain is conserved across species. We show that all seven proteins that contain this domain in yeast localize to one of three MCSs. Human proteins with SMP domains also localize to MCSs when expressed in yeast. The SMP domain binds membranes and is necessary for protein targeting to MCSs. Proteins containing this domain could be involved in lipid metabolism. This is the first protein domain found exclusively in proteins at MCSs.

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