rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
1988-8-8
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pubmed:abstractText |
Placental alkaline phosphatase (PLAP) is anchored to the plasma membrane by a phosphatidylinositol-glycan (PI-G) moiety. During processing of nascent PLAP, a 29-residue COOH-terminal peptide is cleaved out and the PI-G moiety is attached to the newly created COOH terminus of the mature protein. To investigate the structural requirements of the COOH terminus of the nascent protein for PI-G tailing and anchoring to the plasma membrane, we have transfected COS cells with wild type and mutant forms of cDNA encoding human prepro-PLAP. Utilizing a series of COOH-terminal deletion mutants of prepro-PLAP, it was found that to be PI-G-tailed the newly synthesized protein must possess an uncharged, predominantly hydrophobic amino acid sequence of a minimal length in the COOH-terminal peptide. While forms of prepro-PLAP with 17 consecutive hydrophobic residues in the terminal sequence yielded PI-G-tailed and membrane-bound products, prepro-PLAP mutants with 13 or fewer of such residues yielded hydrophilic proteins that were no longer PI-G-tailed but efficiently secreted into the medium. Studies using cassette mutants demonstrated that the precise amino sequence of the COOH-terminal region could be altered as long as minimal hydrophobicity and length was maintained.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alkaline Phosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosylphosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Myristic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Myristic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Palmitic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Palmitic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
263
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10016-21
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:3290206-Alkaline Phosphatase,
pubmed-meshheading:3290206-Amino Acid Sequence,
pubmed-meshheading:3290206-Animals,
pubmed-meshheading:3290206-Base Sequence,
pubmed-meshheading:3290206-Cell Line, Transformed,
pubmed-meshheading:3290206-DNA,
pubmed-meshheading:3290206-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:3290206-Enzyme Precursors,
pubmed-meshheading:3290206-Female,
pubmed-meshheading:3290206-Fluorescent Antibody Technique,
pubmed-meshheading:3290206-Glycosylphosphatidylinositols,
pubmed-meshheading:3290206-Humans,
pubmed-meshheading:3290206-Immunosorbent Techniques,
pubmed-meshheading:3290206-Membrane Proteins,
pubmed-meshheading:3290206-Molecular Sequence Data,
pubmed-meshheading:3290206-Myristic Acid,
pubmed-meshheading:3290206-Myristic Acids,
pubmed-meshheading:3290206-Palmitic Acid,
pubmed-meshheading:3290206-Palmitic Acids,
pubmed-meshheading:3290206-Phosphatidylinositols,
pubmed-meshheading:3290206-Placenta,
pubmed-meshheading:3290206-Polysaccharides,
pubmed-meshheading:3290206-Pregnancy,
pubmed-meshheading:3290206-Transfection
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pubmed:year |
1988
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pubmed:articleTitle |
COOH-terminal requirements for the correct processing of a phosphatidylinositol-glycan anchored membrane protein.
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pubmed:affiliation |
Roche Institute of Molecular Biology, Roche Research Center, Nutley, New Jersey 07110.
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pubmed:publicationType |
Journal Article
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