Title : Kindlin-2 links mechano-environment to proline synthesis and tumor growth.

Pub. Date : 2019 Feb 19

PMID : 30783087






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 We show here that a fraction of kindlin-2 localizes to mitochondria and interacts with pyrroline-5-carboxylate reductase 1 (PYCR1), a key enzyme for proline synthesis. Proline pyrroline-5-carboxylate reductase 1 Homo sapiens
2 We show here that a fraction of kindlin-2 localizes to mitochondria and interacts with pyrroline-5-carboxylate reductase 1 (PYCR1), a key enzyme for proline synthesis. Proline pyrroline-5-carboxylate reductase 1 Homo sapiens
3 Extracellular matrix (ECM) stiffening promotes kindlin-2 translocation into mitochondria and its interaction with PYCR1, resulting in elevation of PYCR1 level and consequent increase of proline synthesis and cell proliferation. Proline pyrroline-5-carboxylate reductase 1 Homo sapiens
4 Our findings reveal a mechanoresponsive kindlin-2-PYCR1 complex that links mechano-environment to proline metabolism and signaling, and suggest a strategy to inhibit tumor growth. Proline pyrroline-5-carboxylate reductase 1 Homo sapiens