Proteomics of the lysosome

Torben Lübke, Peter Lobel, David E. Sleat

Research output: Contribution to journalReview articlepeer-review

207 Scopus citations


Defects in lysosomal function have been associated with numerous monogenic human diseases typically classified as lysosomal storage diseases. However, there is increasing evidence that lysosomal proteins are also involved in more widespread human diseases including cancer and Alzheimer disease. Thus, there is a continuing interest in understanding the cellular functions of the lysosome and an emerging approach to this is the identification of its constituent proteins by proteomic analyses. To date, the mammalian lysosome has been shown to contain ∼ 60 soluble luminal proteins and ∼ 25 transmembrane proteins. However, recent proteomic studies based upon affinity purification of soluble components or subcellular fractionation to obtain both soluble and membrane components suggest that there may be many more of both classes of protein resident within this organelle than previously appreciated. Discovery of such proteins has important implications for understanding the function and the dynamics of the lysosome but can also lead the way towards the discovery of the genetic basis for human diseases of hitherto unknown etiology. Here, we describe current approaches to lysosomal proteomics and data interpretation and review the new lysosomal proteins that have recently emerged from such studies.

Original languageEnglish (US)
Pages (from-to)625-635
Number of pages11
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Issue number4
StatePublished - Apr 2009

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology


  • Lysosomal protein
  • Lysosomal storage disease
  • Mannose-6 phosphate receptor
  • Mass spectrometry
  • Proteomic
  • subcellular fractionation


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