Find protein-protein or protein-gen interaction in the following text.
Determine the interaction type if possible.
Present the found interaction partners in the following form:
partner1 ->-interaction type-> partner2 \n
partner1 and partner 2 should be as short as possible.
DO not forget the "->" and "\n" symbols for every interactions.

An example for the task is given below.
Text:
Heat shock proteins (HSPs) function as molecular chaperones and are key components responsible for protein folding, assembly, translocation, and degradation under stress conditions. However, little is known about how HSPs stabilize proteins and membranes in response to different hormonal or environmental cues in plants. Here, we combined molecular, biochemical, and genetic approaches to elucidate the involvement of cytosolic HSP70-3 in plant stress responses and the interplay between HSP70-3 and plasma membrane (PM)-localized phospholipase Dδ (PLDδ) in Arabidopsis (Arabidopsis thaliana). Analysis using pull-down, coimmunoprecipitation, and bimolecular fluorescence complementation revealed that HSP70-3 specifically interacted with PLDδ. HSP70-3 bound to microtubules, such that it stabilized cortical microtubules upon heat stress. We also showed that heat shock induced recruitment of HSP70-3 to the PM, where HSP70-3 inhibited PLDδ activity to mediate microtubule reorganization, phospholipid metabolism, and plant thermotolerance, and this process depended on the HSP70-3-PLDδ interaction. Our results suggest a model whereby the interplay between HSP70-3 and PLDδ facilitates the re-establishment of cellular homeostasis during plant responses to external stresses and reveal a regulatory mechanism in regulating membrane lipid metabolism. 
Interactions:
HSP70-3->interaction->Dδ
#Task
Text:
Classical DNAJ proteins are co-chaperones that together with HSP70s control 
protein homeostasis. All three classical types of DNAJ proteins (DNAJA, DNAJB 
and DNAJC types) possess the J-domain for interaction with HSP70. DNAJA proteins 
contain, in addition, both the zinc-finger motif and the C-terminal domain which 
are involved in substrate binding, while DNAJB retains only the latter and DNAJC 
comprises only the J-domain. There is increasing evidence that some of the 
activities of DNAJ proteins do not require the J-domain, highlighting the 
functional significance of the other two domains. Indeed, the so-called 
DNAJ-like proteins with a degenerate J-domain have been previously coined as 
DNAJD proteins, and also proteins containing only a DNAJ-like zin