Cloning of the bovine 215-kDa cation-independent mannose 6-phosphate receptor

Insights

Researchers identified partial cDNA sequences for the cation-independent mannose 6-phosphate receptor. This key protein is involved in cellular transport and has a complex structure with homologous repeats.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • The cation-independent mannose 6-phosphate receptor (CI-MPR) is crucial for lysosomal enzyme targeting.
  • Understanding the CI-MPR's structure is vital for elucidating its function in cellular trafficking.

Purpose of the Study:

  • To identify and characterize cDNA clones encoding a partial sequence of the 215-kDa CI-MPR.
  • To analyze the deduced amino acid sequence and structural features of the receptor.

Main Methods:

  • Screening a fetal calf liver cDNA library using oligonucleotide probes.
  • RNA hybridization analysis to determine mRNA length.
  • DNA sequencing to analyze cDNA clones and deduce the amino acid sequence.

Main Results:

  • Four overlapping cDNA clones encoding a partial CI-MPR sequence were identified.
  • The mRNA is approximately 9.5 kilobases, and the sequenced region spans 4647 nucleotides.
  • The deduced polypeptide contains a cytoplasmic domain, a transmembrane segment, and an extracellular domain with eight homologous repeats, including a fibronectin-like segment.

Conclusions:

  • The study provides significant insights into the structural organization of the CI-MPR.
  • The identified repeats and conserved cysteine-bordered units suggest potential functional importance in receptor activity.

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