1. Arimura and Kaibuchi Nature Reviews Neuroscience 8, 194–205 (March 2007) | doi:10.1038/nrn2056

6. Rho GTPase effectors implicated in actin and microtubule dynamics
Rho GTPase effectors implicated in actin and microtubule dynamics. See main text for explanation. (Toca-1) Transducer of Cdc42- dependent actin assembly; (WIP) WASP-interacting protein; (WASP) Wiskott-Aldrich-syndrome protein; (Arp2/3) actin-related proteins 2 and 3; (PAK) p21-activated kinases; (LIMK) Lin-11, Isl-1, and Mec-3 kinase; (Cdk5) cyclin-dependent kinase 5; (IRSp53) insulin receptor substrate of 53 kDa; (Mena) mammalian Ena (Enabled); (WAVE) WASP family Verprolin-homologous protein; (CYFIP) cytoplasmic FMR1-interacting protein; (PIR121) a p53-inducible mRNA; (Nap125) Nck-associated protein; (Abi2) Abl interactor 2; (HSPC) heat-shock protein C; (MLCK) myosin light chain kinase; (MLC) myosin light chain; (MLCP) myosin light chain phosphatase; (Dia) Diaphanous- related formins.
Govek E et al. Genes Dev. 2005;19:1-49

7. La crescita di un neurite è determinata dall’apposizione di nuovi elementi citoscheletrici e di membrana
La direzione di crescita dalla polimerizzazione/depolimerizzazione della actina del GC

12. Rho GTPase signaling downstream of four axon guidance cue families, the semaphorins, ephrins, netrins, and slit proteins
Rho GTPase signaling downstream of four axon guidance cue families, the semaphorins, ephrins, netrins, and slit proteins. These guidance cues are read by growth cone receptors, and signal transduction pathways downstream of these receptors converge onto the Rho GTPases to elicit changes in cytoskeletal organization that determine which way the growth cone will turn. See text for explanations. (Sema) Semaphorin; (Met) hepatocyte growth factor receptor; (LARG) leukemia-associated Rho GEF; (PAK) p21- activated kinases; (Nrp-1) neuropilin-1; (Fyn) Src family kinase; (Cdk5) cyclin-dependent kinase 5; (LIMK) Lin-11, Isl-1, and Mec-3 kinase; (Robo) Roundabout; Dock Dreadlocks; (srGAP1) Slit–Robo GAP 1; (DCC) deleted in colorectal cancer; (UNC5) uncoordinated 5.
Govek E et al. Genes Dev. 2005;19:1-49
©2005 by Cold Spring Harbor Laboratory Press

13. Arimura and Kaibuchi Nature Reviews Neuroscience 8, 194–205 (March 2007) | doi:10.1038/nrn2056

14. Figure 1. ﾊStructure of neurexins and neuroligins
Figure 1.ﾊStructure of neurexins and neuroligins. In humans, there are three neurexin genes and five neuroligin genes. Each neurexin gene uses an upstream promoter to generate the larger α-neurexins and a downstream promoter to generate the smaller β-neurexins. Thus, β-neurexins can be thought of as N-terminally truncated α-neurexins that have a short β-specific leader (βN). In α-neurexins, the LNS (laminin, neurexin, sex-hormone-binding protein) domains are organized with EGF (epidermal growth-factor)-like domains into three homologous modules, IﾐIII. The position of each of five sites of alternative splicing (SS1ﾐSS5) is indicated. Neuroligins contain an extracellular acetylcholinesterase (AChE)-homologous domain that contains one or two sites of alternative splicing (SSA, plus SSB in the case of neuroligin 1). Both neurexins and neuroligins contain a highly glycosylated region (CH) and a transmembrane domain (TM; not present in some splice variants of neurexin 3), and terminate in PDZ-domain-binding sites (PDZ BD). Shown between the neurexins and neuroligins are structures of AChE, a model for the AChE-homologous domain of neuroligins, and the neurexin 1β LNS domain [7]. The position of splice sites SS2ﾐSS4 is shown on a single LNS domain for simplicity, although SS2 and SS3 actually occur in different LNS domains of α-neurexins. Note also that the left face of the neurexin LNS as shown here binds neuroligin [9･･] but the precise structure and interacting region of neuroligin has not been reported yet. The structure files E.C (AChE) and d1c4ra (neurexin LNS) were downloaded from the Research Collaboratory for Structural Bioinformatics protein data bank ( and visualized using the program Visual Molecular Dynamics [66].