Month: September 2012

FLCN phosphorylation was first identified by Baba et al. (2006) when multiple FLCN bands were seen on Western blots. Subsequent studies identified and characterised Serine 62 (S62) and Serine 302 (S302) as phosphorylated residues (Wang et al., 2010; Piao et al., 2009). A third FLCN phosphorylation site, Serine 73 (S73) was identified in a large … Read more

The identification of the FLCN interacting proteins FNIP1 and FNIP2 led to the discovery that FLCN functions in the AMPK signalling pathway (Baba et al., 2006; Hasumi et al., 2008; Takagi et al., 2008). Nahorski et al. (2012) have now identified Plakophilin-4 (PKP4, also known as p0071) as a novel FLCN interactor, and this has … Read more

Mutations in TSC1 and TSC2 are involved in the development of tuberous sclerosis complex (TSC) and lymphangioleiomyomatosis (LAM). These two proteins are thought to function as a heterodimer, where TSC1 stabilises TSC2 and enhances its GTPase-activating protein (GAP) activity. It is this activity which stimulates the small GTPase Rheb, switching it from its mTORC1-activating (GTP-bound) state to its inactive (GDP-bound) state. For more information, do … Read more

Kinesin-1 is a motor protein that is made up of two kinesin heavy chains (KHCs) – which are responsible for the motor activity of the complex, and two kinesin light chains (KLCs) – which bind cargo in many cases. This complex moves along microtubules to transport components, such as vesicles, mitochondria, and even viruses in … Read more