Journal
JOURNAL OF CELL SCIENCE
Volume 128, Issue 5, Pages 979-991Publisher
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.161463
Keywords
Cavin1; Cavin3; Caveolin1; Caveolae; EHD2
Categories
Funding
- Swedish Cancer Society
- Swedish Research Council
- Swedish Foundation for Strategic Research
- Kempe foundation
- Molecular Infection Medicine Sweden (MIMS)
Ask authors/readers for more resources
Caveolae are invaginations of the cell surface thought to regulate membrane tension, signalling, adhesion and lipid homeostasis owing to their dynamic behaviour ranging from stable surface association to dynamic rounds of fission and fusion with the plasma membrane. The caveolae coat is generated by oligomerisation of the membrane protein caveolin and the family of cavin proteins. Here, we show that cavin3 (also known as PRKCDBP) is targeted to caveolae by cavin1 (also known as PTRF) where it interacts with the scaffolding domain of caveolin1 and promote caveolae dynamics. We found that the N-terminal region of cavin3 binds a trimer of the cavin1 N-terminus in competition with a homologous cavin2 (also known as SDPR) region, showing that the cavins form distinct subcomplexes through their N-terminal regions. Our data shows that cavin3 is enriched at deeply invaginated caveolae and that loss of cavin3 in cells results in an increase of stable caveolae and a decrease of caveolae that are only present at the membrane for a short time. We propose that cavin3 is recruited to the caveolae coat by cavin1 to interact with caveolin1 and regulate the duration time of caveolae at the plasma membrane.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available