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. 2019 Mar;9(3):a031500. doi: 10.1101/cshperspect.a031500

Figure 5.

Figure 5.

Interaction partners of neurofibromin. Domain scheme of neurofibromin with reported interaction partners and structurally validated domains colored. Red dots at the bottom part of the scheme indicate nontruncating mutations found in patients and blue and yellow dots on the top part of the scheme represent potential phosphorylation sites for protein kinase A (PKA) and protein kinase C (PKC), respectively. Two ubiquitination sites are indicated as green boxes. Several potential caveolin-binding domains (CBDs) are also indicated. The GAP-related domain (GRD) part indicated in dark red is the minimal GAP domain required for the GAP activity and binds to Ras. Amino-terminal and carboxy-terminal extensions, indicated in light green are overlapping with the tubulin-binding region and the Sec14-PH domain, respectively, and interact with the Sprouty-related protein with an EVH1 domain 1 (Spred1). DDAH1, dimethylarginine dimethylaminohydrolase 1; LRPPRC, leucine-rich pentatricopeptide repeat-containing protein; APP, amyloid precursor protein; FAF2, Fas-associated factor 2; ETEA, expressed in T cells and eosinophils in atopic dermatitis; VCP, valosin-containing protein; LIMK2, LIM domain kinase 2; DPYSL2, dihydropyrimidinase-related protein 2; CRMP2/4, collapsin response mediator protein 2/4; SCF, Skp-Cullin-F box-containing complex; FAK, focal adhesion kinase; CASK, calcium/calmodulin-dependent serine protein kinase (see text).