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Gene Review

PHLDB2  -  pleckstrin homology-like domain, family B,...

Homo sapiens

Synonyms: FLJ21791, LL5B, LL5b, LL5beta, Pleckstrin homology-like domain family B member 2, ...
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High impact information on PHLDB2

  • This interaction could co-localize heterologously expressed gamma-filamin with GFP-LL5beta in the unidentified vesicles [1].
  • Importantly, pleckstrin homology domain mutants of LL5beta that could not bind PtdIns(3,4,5)P(3) were constitutively localized to this vesicle population [1].
  • In addition, expression of platelet-derived growth factor-receptor mutants unable to activate type 1A phosphoinositide 3-kinase (PI3K) or serum starvation in porcine aortic endothelial cells lead to redistribution of LL5beta to this vesicle population [1].
  • Strikingly, a substantial proportion of LL5beta became associated with an unidentified intracellular vesicle population in the context of low PtdIns(3,4,5)P(3) levels produced by the addition of wortmannin or LY294002 [1].
  • Three of the novel proteins (TMEM16A, PHLDB2 and ARHGAP21) were analysed further to show that they have the potential to be developed as therapeutic targets [2].

Biological context of PHLDB2

  • LL5beta is a phosphatidylinositol-3,4,5-triphosphate (PIP3) binding protein, and its recruitment to the cell cortex is influenced by PI3 kinase activity but does not require intact microtubules [3].

Anatomical context of PHLDB2

  • CLASPs attach microtubule plus ends to the cell cortex through a complex with LL5beta [3].
  • LL5beta is required for cortical CLASP accumulation and microtubule stabilization in HeLa cells, while ELKS plays an accessory role in these processes [3].
  • Cortical clusters of LL5beta and ELKS do not overlap with focal adhesions but often form in their vicinity and can affect their size [3].
  • Work in this issue of Developmental Cell identifies the protein LL5beta as a key CLASP binding platform that mediates communication between the cell cortex and the microtubule cytoskeleton [4].
  • LL5beta and ELKS form a complex that colocalizes with CLASPs at the cortex of HeLa cells as well as at the leading edge of motile fibroblasts [3].


  1. LL5beta is a phosphatidylinositol (3,4,5)-trisphosphate sensor that can bind the cytoskeletal adaptor, gamma-filamin. Paranavitane, V., Coadwell, W.J., Eguinoa, A., Hawkins, P.T., Stephens, L. J. Biol. Chem. (2003) [Pubmed]
  2. Head and neck squamous cell carcinoma transcriptome analysis by comprehensive validated differential display. Carles, A., Millon, R., Cromer, A., Ganguli, G., Lemaire, F., Young, J., Wasylyk, C., Muller, D., Schultz, I., Rabouel, Y., Dembélé, D., Zhao, C., Marchal, P., Ducray, C., Bracco, L., Abecassis, J., Poch, O., Wasylyk, B. Oncogene (2006) [Pubmed]
  3. CLASPs attach microtubule plus ends to the cell cortex through a complex with LL5beta. Lansbergen, G., Grigoriev, I., Mimori-Kiyosue, Y., Ohtsuka, T., Higa, S., Kitajima, I., Demmers, J., Galjart, N., Houtsmuller, A.B., Grosveld, F., Akhmanova, A. Dev. Cell (2006) [Pubmed]
  4. CLASPing the cell cortex. Goodson, H.V., Folker, E.S. Dev. Cell (2006) [Pubmed]
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