Lack of palmitoylation redirects p59Hck from the plasma membrane to p61Hck-positive lysosomes.

doi:10.1074/jbc.M003901200

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

Lack of palmitoylation redirects p59Hck from the plasma membrane to p61Hck-positive lysosomes.

The Journal of biological chemistry - 17 Nov 2000

Carréno S, Gouze M E, Schaak S, Emorine L J, Maridonneau-Parini I

Abstract excerpt

Hck, a protein-tyrosine kinase of phagocytes, is the unique member of the Src family expressed under two alternatively translated isoforms differing in their N-terminal site of acylation: p61(Hck) has an additional 21-amino acid sequence comprising a single myristoylation motif, whereas p59(Hck) N terminus has myristoylation and palmitoylation sites. To identify the molecular determinants involved in the...

Topics

Animals
CHO Cells
Cell Membrane
Cricetinae
Genes, Reporter
Golgi Apparatus
HeLa Cells
Humans
Lysosomes
Membrane Proteins
Microscopy, Fluorescence
Mutation
Palmitic Acid
Protein Isoforms
Protein Structure, Tertiary

Source

Open in PubMed

Identifiers

PMID: 10967098
DOI: 10.1074/jbc.M003901200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Transport

Protein-Tyrosine Kinases

Proto-Oncogene Proteins